FORTY-FOUR YEARS (1955–1999) DEVOTED TO HEMOGLOBIN RESEARCH: TITUS H. J. HUISMAN (1923–1999)

PUBLICATIONS SELECTED FROM A TOTAL OF 913

• McDonald C. D., Jr., Huisman T. H.J. The application of agar-gel electrophoresis according to Wiemeto the identification of hemoglobin types. Clin. Chim. Acta 1963; 8: 639–640
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Jonxis J. H.P. The Hemoglobinopathies Techniques ofIdentification. MarcelDekker, Inc., New York, NY, USA 1997; 6, Clinical and Biochemical Analysis
   Google Scholar
• Gravely M. E., Altay C., Huisman T. H.J. Misdiagnosis of combinations of Hb S and other β-chainabnormal hemoglobins using a simple electrophoretic procedure. Lab. Med. 1981; 12: 499–502
   Google Scholar
• Huisman T. H.J. Introduction and review of standard methodology for the detection of hemoglobin abnormalities. The Hemoglobinopathies, T. H.J. Huisman, ChurchillLivingstone, Edinburgh, Scotland 1986; 15: 1–31, Methods in Hematology
   Google Scholar
• Huisman T. H.J., Dozy A. M. Studies on the heterogeneity of hemoglobin. IX. the use of tris(hydroxymethyl)aminomethane-HClbuffers in the anion-exchange chromatography of hemoglobins. J. Chromatogr 1965; 19: 160–169
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Studies on the heterogeneity of hemoglobin. XI. chromatographicstudies on intermediate forms of Oxy- and ferrihemoglobin. Arch. Biochem. Biophys 1966; 113: 427–434
   PubMed Web of Science ®Google Scholar
• Dozy A. M., Kleihauer E. F., Huisman T. H.J. Studies on the heterogeneity of hemoglobin. XIII. chromatographyof various human and animal hemoglobin types on DEAE-Sephadex. J. Chromatogr 1968; 32: 723–727
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M. Studies on the heterogeneity of hemoglobin. IV. chromatographicbehavior of different human hemoglobins in anion-exchange chromatography (DEAE-cellulose). J. Chromatogr. 1962; 7: 180–203
   Web of Science ®Google Scholar
• Efremov G. D., Huisman T. H.J. Studies on the heterogeneity of hemoglobin. XV. separation offetal hemoglobin and the normally occurring minor adult hemoglobins by chromatographyon DEAE-cellulose. J. Chromatogr. 1974; 89: 191–196
   Web of Science ®Google Scholar
• Huisman T. H.J., Schroeder W. A., Stamatoyannopoulos G., Bouver N., Shelton J. R., Shelton J. B., Apell G. Nature of fetal hemoglobin in the Greek type of hereditary persistenceof fetal hemoglobin with and without concurrent β-thalassemia. J. Clin. Invest. 1970; 49: 1035–1040
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. (1980) Abnormalities in Hemoglobin andRed Cell Enzymes, Section A: Hemoglobin and Its Abnormalities Chromatographicmethods for the separation of normal and abnormal hemoglobins. Proceedings of the U.S.–Japan CooperativeScience Program, Honolulu, HI, USA, January, 14–181980, 527–539, 4 (3&4) Hemoglobin
   Google Scholar
• Abraham E. C., Reese A., Stallings M., Huisman T. H.J. Separation of Human hemoglobins by DEAE-cellulose chromatographyusing glycine-KCN-NaCl developers. Hemoglobin 1977; 1(1)27–44
   Web of Science ®Google Scholar
• Dozy A. M., Huisman T. H.J. Studies on the heterogeneity of hemoglobin. XIV. chromatographyof normal and abnormal human hemoglobin types on CMsephadex. J. Chromatogr. 1969; 40: 62–70
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Chromatographic separation of hemoglobins A2 and C. The quantitiesof hemoglobin A2 in patients with AC trait, CC disease, and C-β-thalassemia. Clin. Chim. Acta 1972; 40: 159–163
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Wrightstone R. N. Studies on the heterogeneity of hemoglobin. XVI. Separationof variants with a Glu→Lys substitution by chromatography on CM-cellulose. J. Chromatogr. 1974; 92: 391–399
   PubMed Web of Science ®Google Scholar
• Henson J. B., Carver J. R., Wilson J. B., Huisman T. H.J. Carboxymethyl-cellulose microchromatography for the quantitationof hemoglobin Bart's (γ4) and its use in the detection of the α-thalassemiaconditions. J. Chromatogr. 1980; 198: 443–448
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M. Quantitative determination of the minor hemoglobin componentHb-A2 by DEAE-cellulose chromatography. Anal. Biochem. 1961; 2: 400–403
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Quantitative determination of Hb-A2 using DEAE-cellulosechromatography. Proceedings ofthe Haemoglobin-Colloquium, ViennaAustria. H. Lehmann, K. Betke. Georg Thieme Verlag, StuttgartGermany 1961; 95–96
   Google Scholar
• Schleider C. T.H., Mayson S. M., Huisman T. H.J. Further modification of the microchromatographic determinationof hemoglobin A2. hemoglobin 1977; 1(5)503–504
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M. Studies on the heterogeneity of hemoglobin. V. binding of hemoglobinwith oxidized glutathione. J. Lab. Clin. Med. 1962; 60: 302–319
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Horton B. F. Studies on the heterogeneity of hemoglobin. VIII. chromatographicand electrophoretic investigations of various minor hemoglobin fractions presentin normal and in vitro modified red blood cell hemolysates. J. Chromatogr. 1965; 18: 116–123
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M., Horton B. F., Nechtman C. M. Studies on the heterogeneity of hemoglobin. X. the nature ofvarious minor hemoglobin components produced in human red blood cell hemolysateson aging. J. Lab. Clin. Med. 1966; 67: 355–373
   PubMed Web of Science ®Google Scholar
• Horton B. F., Huisman T. H.J. Studies on the heterogeneity of haemoglobin. VII. minor haemoglobincomponents in haematological diseases. Br. J. Haematol. 1965; 11: 296–304
   PubMed Web of Science ®Google Scholar
• Mobley R., Huisman T. H.J. Minor hemoglobins (Hb A1) in chronic alcoholic patients. Hemoglobin 1982; 6(1)79–81
   PubMed Web of Science ®Google Scholar
• Boyd E. M., Thomas D. R., Horton B. F., Huisman T. H.J. The quantities of various minor hemoglobin components in oldand young human red blood cells. Clin. Chim. Acta 1967; 16: 333–341
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Huisman T. H.J. On the quaternary structure of hemoglobin AIc. Biochim. Biophys. Acta 1969; 194: 609–611
   PubMedGoogle Scholar
• Bakioglu I., Kutlar A., Huisman T. H.J. Differences between the levels of Gγchain in the fetal hemoglobin of two types of HPFH are linked with a variationin the DNA sequence. Biochem. Genet. 1986; 24: 149–151
   PubMed Web of Science ®Google Scholar
• Alter B. P., Goff S. C., Efremov G. D., Gravely M. E., Huisman T. H.J. Globin chain electrophoresis: a new approach to the determinationof the Gγ/Aγratio in fetal haemoglobin and to studies of globin synthesis. Br. J. Haematol. 1980; 44: 527–534
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Markovska B., Stojanovski N., Petkov G., Nikolov N., Huisman T. H.J. The use of globin chain electrophoresis in polyacrylamide gelsfor the quantitation of the Gγ to Aγratio in fetal hemoglobin. Hemoglobin 1981; 5(7&8)637–651
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Lam H., Pravatmuang P., Huisman T. H.J. Separation of the tryptic peptides of normal and abnormal α,β, γ, and δ hemoglobin chains by highperformance liquid chromatography. J. Chromatogr. 1979; 179: 271–290
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Chen S. S., Webber B. B., Kutlar A., Kutlar F., Villegas A., Huisman T. H.J. The identification of five rare β-chain abnormal hemoglobinsby high performance liquid chromatographic procedures. Hemoglobin 1986; 10(1)49–63
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Burnley M. S., Huisman T. H.J. Fetal hemoglobin variants identified in adults through restrictionendonuclease gene mapping methodology. Blood 1985; 66: 803–807
   PubMed Web of Science ®Google Scholar
• Li H-W., Codrington J. F., Schiliro G., Wadsworth L. D., Beris Ph., Adekile A. D., Huisman T. H.J. The usefulness of sequence analysis of amplified DNA for theidentification of δ chain variants. Hemoglobin 1991; 15(1)77–84
   PubMed Web of Science ®Google Scholar
• Postnikov Yu. V., Molchanova T. P., Huisman T. H.J. Allele-specific amplification for the identification of severalhemoglobin variants. Hemoglobin 1993; 17(5)439–452
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Webber B. The frequency of the AγTgene in the presence and absence of the βSor βC gene in the black population of thesoutheastern USA. Hemoglobin 1981; 5(5)441–451
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Kutlar F., Nakatsuji T., Bruce-Tagoe A., Kilinć Y., Cauchi M. N., Romero Garcia C. The frequency of the g chain variant AgT in different populations,and its use in evaluating g gene expression in association with thalassemia. Hum. Genet. 1985; 71: 127–133
   PubMed Web of Science ®Google Scholar
• Gu L-H., Öner C., Huisman T. H.J. The GγTchain (gene conversion and that in Hb F-Waynesboro of a mutated Gγgene. Hemoglobin 1995; 19(6)413–418
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Abraham B. L., Harris H. F., Gravely M. E., Henson J., Williams D., Wilson J. B., Miller A., Mayson S., Wrightstone R. N., Moss E., Joseph B., Walker L., Brisco J., Brisco L. (1980) Hemoglobinopathiesobserved in the population of the Southeastern United States (SE-USA) In Abnormalitiesin Hemoglobin and Red Cell Enzymes, Section A: Hemoglobin and Its Abnormalities. Proceedings of the U.S.-Japan Cooperative ScienceProgram, Honolulu, HI, USA, January, 14–181980. 4 (3&4): 373–386, Hemoglobin
   Google Scholar
• Huisman T. H.J., Harris H. F., Stewart A., Kutlar A., Gardner R. J., Green C. The frequencies of the Hbs S and C in blacks living in the coastalareas of Georgia and South Carolina. Hum. Genet. 1991; 87: 102–103
   PubMed Web of Science ®Google Scholar
• Ojwang P. J., Ogada T., Bakioglu I., Headlee M. G., Reese A. L., Huisman T. H.J. Abnormal human haemoglobins in Western Kenya. E. Afr. Med. J. 1984; 61: 886–891
   PubMed Web of Science ®Google Scholar
• Ojwang P. J., Ogada T., Gonzalez-Redondo J. M., Kutlar A., Kutlar F., Huisman T. H.J. βS-Haplotypes and a-thalassaemiaalong the coastal belt of Kenya. E. Afr. Med. J. 1989; 66: 377–380
   PubMed Web of Science ®Google Scholar
• Rachmilewitz E. A., Levi S., Huisman T. H.J. High frequency of haemoglobin C in an Israel Bedouin tribe. J. Med. Sci. 1974; 10: 219–224
   Google Scholar
• Brittenham G., Lozoff B., Harris J. W., Mayson S. M., Miller A., Huisman T. H.J. Sickle cell anemia and trait in Southern India: further studies. Am. J. Hematol 1979; 6: 107–123
   PubMed Web of Science ®Google Scholar
• Gupta R. B., Tiwary R. S., Pande P. L., Kutlar F., Oner C., Oner R., Huisman T. H.J. Hemoglobinopathies among the Gond tribal groups of Central India;interactions of a- and β-thalassemia with b chain variants. Hemoglobin 1991; 15(5)441–458
   PubMed Web of Science ®Google Scholar
• Li H-J., Qin F., Li H-W., Li L., He X-J., Chang X-S., Zhao X-N., Li Z-M., Liang K-X., Xing F-L., Chang W-S., Wong R-Z., Yang I-L., Li F-S., Zhang T-T., Tian R-J., Webber B. B., Wilson J. B., Huisman T. H.J. Abnormal hemoglobins in the silk road region of China. Hum. Genet. 1990; 86: 231–235
   PubMed Web of Science ®Google Scholar
• Zhao W., Wilson J. B., Huisman T. H.J. Low quantities of Hb Boyle Heights or α26(A4)Asp→0β2observed in three members of a Caucasian family. Hemoglobin 1990; 14(6)637–640
   PubMed Web of Science ®Google Scholar
• Pobedimskaya D. D., Molchanova T. P., Streichman S., Huisman T. H.J. Compound heterozygosity for two α-globin gene defects,Hb Taybe (α1; 38 or 39 minus Thr) and a poly A mutation (α2; AATAAA→AATAAG),results in a severe hemolytic anemia. Am. J. Hematol. 1994; 47: 198–202
   PubMed Web of Science ®Google Scholar
• Jones R. T., Brimhall B., Huisman T. H.J., Kleihauer E., Betke E. Hemoglobin Freiburg: abnormal hemoglobin due to a deletion ofa single amino acid residue. Science 1966; 154: 1024–1027
   PubMed Web of Science ®Google Scholar
• Kamel K., El-Najjar A., Webber B. B., Chen S. S., Wilson J. B., Kutlar A., Huisman T. H.J. Hb Doha or α2β2[X-N-Met-1(NA1)Val→Glu]; a newβ chain abnormal hemoglobin observed in a Qatari femal. Biochim. Biophys. Acta 1985; 831: 257–260
   PubMed Web of Science ®Google Scholar
• Jogessar V. B., Westermeyer K., Webber B. B., Wilson J. B., Hu H., Gonzalez- Redondo J. M., Kutlar A., Huisman T. H.J. Hb Natal or α2(minus Tyr-Arg)β2, a high oxygen affinitya chain variant with a deleted carboxy-terminus resulting from a TAC→TAA(Tyr→terminating codon) mutation in codon α140. Biochim.Biophys. Acta 1988; 951: 36–41
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Headlee M. G., Wilson J. B., Lam H., Johnson S. E.N., Webber B. B.Hb Wayne. The frameshift variant with extended a chains observed in aCaucasian family from Alabama. Hemoglobin 1984; 8(1)1–15
   PubMed Web of Science ®Google Scholar
• Salkie M. L., Higgins T., Morrison D. M., Wilson J. B., Gu L-H., Curuk M. A., Baysal E., Huisman T. H.J. A Canadian family with Hb Wayne; characterization by HPLC andDNA sequencing. Hemoglobin 1992; 16(6)515–519
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Wilson J. B., Gravely M., Hubbard M. Hemoglobin Grady: the first example of a variant with elongatedchains due to an insertion of residues. Proc. Natl. Acad. Sci. USA 1974; 71: 3270–3273
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Miller A. Hb Grady and a Thalassemia: a contribution to the problem ofthe number of Hba structural loci in man. Am. J. Hum. Genet. 1976; 28: 363–369
   PubMed Web of Science ®Google Scholar
• Cleek M. P., Gardiner M. B., Reese A. L., Harris H. F., Felice A. E., Huisman T. H.J. The Atlanta family with hemoglobin Grady revisited. Am. J. Hum. Genet. 1983; 35: 1314–1316
   PubMed Web of Science ®Google Scholar
• Plaseska D., Dimovski A. J., Wilson J. B., Webber B. B., Hume H. A., Huisman T. H.J. Hemoglobin Montreal, a new variant with an extended b chaindue to a deletion of Asp, Gly, Leu at positions 73, 74, and 75, and an insertionof Ala, Arg, Cys, and Gln at the same location. Blood 1991; 77: 178–181
   PubMed Web of Science ®Google Scholar
• Murari J., Smith L. L., Wilson J. B., Schneider R. G., Huisman T. H.J. Some properties of hemoglobinl. Hemoglobin 1977; 1(2)267–282
   PubMedGoogle Scholar
• Prchal J. T., Hall K. M., de Pablos J. Ma, Rodriguez I., Huisman T. H.J. Hb Birmingham and Hb Galicia; two unstable β chain variantscharacterized by small deletions and insertion. Blood 1990; 75: 1883–1887
   PubMed Web of Science ®Google Scholar
• Altay C., Niazi G. A., Huisman T. H.J. The combination of Hb S and Hb E in a black female. Hemoglobin 1977; 1(1)100–102
   Web of Science ®Google Scholar
• Duerr M., Gross S., Ramachandran M., Huisman T. H.J. Case report: Hb CE disease in a 5–year-old without clinicalsymptoms. Hematol. Revs. 1991; 5: 141–142
   Google Scholar
• Gu L-H., Leonova J. Ye., Huisman T. H.J. Hb S-Hb Lufkin disease in a black male infant. Hemoglobin 1995; 19(5)291–294
   PubMed Web of Science ®Google Scholar
• Brittenham G., Lozoff B., Harris J. W., Nayudu N. V.S., Gravely M., Wilson J. B., Lam H., Huisman T. H.J. Hemoglobin Hofu or α2β2 [126(H4)Val→Glu] foundin combination with hemoglobin S. Hemoglobin 1978; 2(6)541–549
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. The hemoglobin P-Galveston-Hb-C condition in members of a blackfamily from South Carolina. FEBS Lett. 1978; 94: 68–72
   PubMed Web of Science ®Google Scholar
• Wong S. C., Huisman T. H.J. Further evidence for non-linkage of the Hbα and Hbβstructural loci in man. Clin. Chim. Acta 1972; 38: 473–474
   PubMed Web of Science ®Google Scholar
• Wrightstone R. N., Hubbard M., Huisman T. H.J. Hemoglobin S-Gα Georgia Ddisease: a case report. Acta Haematol. 1974; 51: 315–320
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Gravely M. E., Wilson J. B., Webber B., Felice A. E., Miller A. Interaction of the b chain variant hemoglobin Leslie and thea chain variant hemoglobin Montgomery in a black female. Am. J. Hematol. 1980; 8: 139–147
   Web of Science ®Google Scholar
• Abraham E. C., Huisman T. H.J. Differences in affinity of variant b chains for a chains: apossible explanation for the variation in the percentages of b chain variantsin heterozygotes. Hemoglobin 1977; 1(8)547–560
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Percentages of abnormal hemoglobins in adults with a heterozygosityfor an α chain and/or a β chain variant. Am. J. Hematol 1983; 14: 393–404
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Gravely M. E., Henson J., Felice A., Wilson J. B., Abraham E. C., Vella F., Little M. W. Variability in the interaction of β-thalassemia with theα-chain variants Hb G-Philadelphia and Hb Rampa. J. Lab. Clin. Med. 1978; 92: 311–320
   PubMed Web of Science ®Google Scholar
• Qin W-B., Baysal E., Wong K. F., Molchanova T. P., Pobedimskaya D. D., Sharma S., Wilson J. B., Huisman T. H.J. The quantities of αQ chain variants in heterozygotes withand without a concomitant β-thalassemia trait. Am. J. Hematol. 1994; 45: 91–93
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Kutlar F., Kutlar A., Stoming T. A., de Pablos J. Ma, Kiliņ Y., Huisman T. H.J. Hb S(C)-β+-thalassaemia: different mutations are associatedwith different levels of normal Hb A. Br. J. Haematol. 1988; 70: 85–89
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Stoming T. A., Kutlar F., Kutlar A., McKie V. C., McKie K. M., Huisman T. H.J. Severe Hb S-β0-thalassaemia with a T→C substitutionin the donor splice site of the first intron of the β-globin gene. Br. J. Haematol 1989; 71: 113–117
   PubMed Web of Science ®Google Scholar
• Divoky V., Baysal E., Schiliro G., Dibenedetto S. P., Huisman T. H.J. A mild type of Hb S-β+-thalassemia [−92 (C→T)]in a Sicilian family. Am. J. Hematol. 1993; 42: 224–226
   Web of Science ®Google Scholar
• Sydenstricker V. P., Horton B., Payne R. A., Huisman T. H.J. Studies on a fast hemoglobin variant found in a Negro familyin association with thalassemia. Clin. Chim. Acta 1961; 6: 677–685
   Web of Science ®Google Scholar
• Lutcher C. L., Wilson J. B., Gravely M. E., Stevens P. D., Chen C. J., Lindeman J. G., Wong S. C., Miller A., Gottlieb M., Huisman T. H.J. Hb Leslie, an unstable hemoglobin due to a deletion of glutaminylresidue β 131 (H9) occurring in association with β0-thalassemia,HbC and HbS. Blood 1976; 47: 99–112
   PubMed Web of Science ®Google Scholar
• Carcassi U. E.F., Pintus A., Gravely M. E., Huisman T. H.J. β0-Thalassemia in association with Hb Leslie (α2β2131 Gln→0) in a Sardinian family. Hemoglobin 1980; 4(2)195–200
   PubMed Web of Science ®Google Scholar
• Milner P. F., Corley C. C., Pomeroy W. L., Wilson J. B., Gravely M., Huisman T. H.J. Thalassemia intermedia caused by heterozygosity for both β-thalassemia and hemoglobin Saki [β14(A11)Leu→Pro]. Am. J. Hematol. 1976; 1: 283–292
   PubMed Web of Science ®Google Scholar
• Divoky V., Bissé E., Wilson J. B., Gu L-H., Wieland H., Heinrichs I., Prior J. F., Huisman T. H.J. Heterozygosity for the IVS-I-5 (G→C) mutation with a G→Achange at codon 18 (Val→Met; Hb Baden) in cis and a T→G mutationat codon 126 (Val→Gly; Hb Dhonburi) in trans resulting in a thalassemiaintermedia. Biochim. Biophys. Acta 1982; 1180: 173–179
   Google Scholar
• Aksoy M., Kutlar A., Kutlar F., Dincol G., Erdem S., Wilson J. B., Huisman T. H.J. Hb Beograd-β0-thalassemia in a Turkish family from Yugoslavia. Hemoglobin 1984; 8(4)417–421
   PubMed Web of Science ®Google Scholar
• Romero C., Fernandez Fuertes I., Quintana A., Blanco L., Navarro J. L., Wilson J. B., Huisman T. H.J. Hb G-Szuhu or α2β280)EF4)Asn→Lys, in combinationwith β0-thalassemia in a Spanish family. Hemoglobin 1985; 9(5)535–539
   PubMed Web of Science ®Google Scholar
• Pinkerton P. H., Wilson J. B., Lam H., Williams D., Huisman T. H.J. Hemoglobin Riyadh-β0-thalassemia in an Indian family. Hemoglobin 1979; 3(6)451–458
   PubMed Web of Science ®Google Scholar
• Pande P. L., Prakash S., Tiwary R. S., Kazanetz E. G., Leonova J. Ye., Huisman T. H.J. β-Thalassemia intermedia in an Indian female with the HbHofu [β126(H4)Val→Glu]-β0-thalassemia [codons 8/9 (+G)] combination. Hemoglobin 1995; 19(5)301–306
   PubMed Web of Science ®Google Scholar
• Gray G. R., Manson H. E., Gu L-H., Leonova J. Ye., Huisman T. H.J. Hb Lulu Island [α2β2107(G9)Gly→Asp]-β0-thalassemia(codon 15; TGG→TAG), a form of thalassemia intermedia. Am. J. Hematol 1995; 50: 26–29
   PubMed Web of Science ®Google Scholar
• Yang K. G., Kutlar F., George E., Wilson J. B., Kutlar A., Stoming T. A., Gonzalez-Redondo J. M., Huisman T. H.J. Molecular characterization of β-globin gene mutations inMalay patients with Hb E-β-thalassaemia and thalassaemia major. Br. J. Haematol 1989; 72: 73–80
   PubMed Web of Science ®Google Scholar
• Labie D., Schroeder W. A., Huisman T. H.J. The amino acid sequence of the δ–β chains ofhemoglobin Lepore Augusta=Lepore Washington. Biochim.Biophys. Acta 1966; 127: 428–437
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Sadikario A., Stojmirovic E., Schroeder W. A., Shelton J. R., Shelton J. B., Apell G., Wilson J. B., Brodie A. R., Huisman T. H.J. Chemical heterogeneity of foetal haemoglobin in the Lepore haemoglobinopathy. Br. J. Haematol 1974; 27: 319–329
   PubMed Web of Science ®Google Scholar
• Efremov D. G., Efremov G. D., Zisovksi N., Stojanovski N., Kutlar F., Diaz- Chico J. C., Kutlar A., Yang K. G., Stoming T. A., Huisman T. H.J. Variation in clinical severity among patients with Lepore-Boston-β-thalassaemiais related to the type of β-thalassaemia. Br. J. Haematol 1988; 68: 351–355
   PubMed Web of Science ®Google Scholar
• Bozkurt G., Baysal E., Gu L-H., Huisman T. H.J. Thalassemia intermedia in two patients with Hb Lepore-β0-thalassemia(frameshift codon 8, –AA). Hemoglobin 1994; 18(3)247–250
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Rudivić R., Niazi G. A., Hunter E. Jr., Huisman T. H.J., Schroeder W. A. An individual with Hb-Lepore-Baltimore-δβ-thalassemiain a Yugoslavian family. Scand. J. Haematol 1976; 16: 81–89
   PubMedGoogle Scholar
• Masala B., Manca L., Wilson J. B., Webber B. B., Kutlar A., Huisman T. H.J. Hb Lepore-Baltimore in a North Sardinian family. Hemoglobin 1990; 14(3)241–246
   PubMed Web of Science ®Google Scholar
• Abu-Sin A., Felice A. E., Gravely M. E., Wilson J. B., Reese A. L., Lam H., Miller A., Huisman T. H.J. Hb P-nilotic in association with β0-thalassemia: cismutationof a hemoglobin βA chain regulatory determinant. J. Lab. Clin. Med. 1979; 93: 973–982
   PubMed Web of Science ®Google Scholar
• Altay Ç, Kutlar A., Wilson J. B., Webber B. B., Huisman T. H.J. Hb P-nilotic or α2(βδ)2 in a Turkish family. Hemoglobin 1987; 11(4)395–399
   PubMed Web of Science ®Google Scholar
• Liu J. Z., Harano T., Lanclos K. D., Huisman T. H.J. The β–δ crossover leading to the βδhybrid gene of Hb P-nilotic is located within 54 base pairs of the 5′end of exon 2 or between codons 31 and 50. Biochim. Biophys. Acta 1987; 909: 208–212
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Wrightstone R. N., Wilson J. B., Schroeder W. A., Kendall A. G. Hemoglobin Kenya, the product of fusion γ and β polypeptidechains. Arch. Biochem. Biophys. 1972; 153: 850–853
   PubMed Web of Science ®Google Scholar
• Kendall A. G., Ojwang P. J., Schroeder W. A., Huisman T. H.J. Hemoglobin Kenya, the produce of a γ−β fusiongene: studies of the family. Am. J. Hum. Genet. 1973; 25: 548–563
   PubMed Web of Science ®Google Scholar
• Ojwang P. J., Nakatsuji T., Gardiner M. B., Reese A. L., Gilman J. G., Huisman T. H.J. Gene deletion as the molecular basis of the Kenya-Gγ-HPFHcondition. Hemoglobin 1983; 7(2)115–123
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Huisman T. H.J., Shelton J. R., Shelton J. B., Kleihauer E. F., Dozy A. M., Robberson B. Evidence for multiple structural genes for the γ chainof human fetal hemoglobin. Proc. Natl. Acad. Sci. USA 1968; 60: 537–544
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. A note on the dissociation of human foetal haemoglobin at lowpH. Biochim. Biophys. Acta 1961; 46: 384–385
   PubMedGoogle Scholar
• Schroeder W. A., Huisman T. H.J., Shelton J. R., Wilson J. B. An improved method for quantitative determination of human fetalhemoglobin. Anal. Biochem. 1970; 35: 235–243
   PubMed Web of Science ®Google Scholar
• Abraham E. C., Reese A., Stallings M., Garver F. A., Huisman T. H.J. An improved chromatographic procedure for quantitation of humanfetal hemoglobin. Hemoglobin 1977; 1(5)547–560
   PubMedGoogle Scholar
• Kutlar A., Kutlar F., Gu L-G., Mayson S. M., Huisman T. H.J. Fetal hemoglobin in normal adults and β-thalassemia heterozygotes. Hum. Genet. 1990; 85: 106–110
   PubMed Web of Science ®Google Scholar
• Stoming T. A., Garver F. A., Gangarosa M. A., Harrison J. M., Huisman T. H.J. Separation of the Aγ and Gγ cyanogen bromide peptidesof human fetal hemoglobin by high-pressure liquid chromatography. Anal. Bioch. 1979; 96: 113–117
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Wilson J. B. Recent advances in the quantitation of human fetal hemoglobinswith different gamma chains. Am. J. Hematol 1980; 9: 225–235
   PubMed Web of Science ®Google Scholar
• Abraham E. C., Cope N. D., Braziel N. N., Huisman T. H.J. On the chromatographic heterogeneity of human fetal hemoglobin. Biochim. Biophys. Acta 1979; 577: 159–169
   PubMed Web of Science ®Google Scholar
• Plaseska D., Gu L-H., Wilson J. B., Codrington J. F., Huisman T. H.J. Hb sun prairie or α2130(H13)Ala→Proβ2; secondobservation in an Indian adult. Hemoglobin 1990; 14(5)491–497
   PubMed Web of Science ®Google Scholar
• Shimizu K., Wilson J. B., Huisman T. H.J. (1980) The determination of the percentagesof Gγ and Aγ; Chain in human fetal hemoglobin by HPLC. Abnormalities in Hemoglobin and Red Cell Enzymes, SectionA: Hemoglobin and Its Abnormalities. Proceedingsof the U.S.–Japan Cooperative Science Program, Honolulu, HI, USA, January, 14–181980. 4 (3&4): 487–496, Hemoglobin
   Google Scholar
• Bakioglu I., Reese A. L., Huisman T. H.J. A comparison of two procedures useful for the isolation of HbF from adult red blood cells and for the quantitation of the types of γchain by high-performance liquid chromatography. J. Chromatogr. 1984; 295: 171–177
   PubMed Web of Science ®Google Scholar
• Kutlar F., Huisman T. H.J. A new ultra-micro high-performance liquid chromatographic methodfor determining the γ chain composition of hemoglobin F in normal adults. J. Chromatogr. 1993; 620: 183–189
   PubMed Web of Science ®Google Scholar
• Horton B. F., Hahn D. A., Huisman T. H.J. Slight increase of fetal hemoglobin in apparently healthy Negroes. Acta Haematol. 1965; 33: 312–319
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Gjorgovski I., Stojanovski N., Diaz-Chico J. C., Harano T., Kutlar F., Huisman T. H.J. One haplotype is associated with the Swiss type of hereditarypersistence of fetal hemoglobin in the Yugoslavian population. Hum. Genet. 1987; 77: 132–136
   PubMed Web of Science ®Google Scholar
• Leonova J. Ye., Kazanetz E. G., Smetanina N. S., Adekile A. D., Efremov G. D., Huisman T. H.J. Variability in the fetal hemoglobin level of the normal adult. Am. J.Hematol. 1996; 53: 59–65
   PubMed Web of Science ®Google Scholar
• Aksoy M., Erdem Ş, Schroeder W. A., Huisman T. H.J. Hemoglobins A2 and F in chronicbenzene poisoning. Proceedingsof the International Symposium on Abnormal Hemoglobins and Thalassemia, IstanbulTurkey, 1974, 197–204
   Google Scholar
• Huisman T. H.J., Schroeder W. A. Fetal hemoglobin synthesis in some forms of leukemia. XXIII Colloquium of the Biological Fluids Bruges, Belgium, 1976. PergamonPress, New York, NY, USA, 547–554
   Google Scholar
• Altay C., Say B., Yetgkin S., Huisman T. H.J. α-Thalassemia and β-thalassemia in a Turkish family. Am. J. Hematol. 1977; 2: 1–15
   PubMed Web of Science ®Google Scholar
• Alter B. P., Rappeport J. M., Huisman T. H.J., Schroeder W. A., Nathan D. G. Fetal erythropoiesis following bone marrow transplantation. Blood 1976; 48: 843–853
   PubMed Web of Science ®Google Scholar
• Kutlar F., Kutlar A., Gu Y. C., Huisman T. H.J. Adult hemoglobin levels in newborn babies from different countriesand in babies with some significant hemoglobinopathies. Acta Haematol 1987; 78: 28–32
   PubMed Web of Science ®Google Scholar
• Hattori Y., Kutlar F., Mosley C. J., Mayson S. M., Huisman T. H.J. Association of the level of Gd chain in the fetal hemoglobinof normal adults with specific haplotypes. Hemoglobin 1986; 10(2)185–204
   PubMed Web of Science ®Google Scholar
• Zielke H. R., Meny R. G., O'Brien M. J., Smialek J. E., Kutlar F., Huisman T. H.J., Dover G. J. Normal fetal hemoglobin levels in the sudden infant death syndrome. N.Engl. J. Med. 1989; 321: 1359–1364
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Huisman T. H.J. Investigation of molecular variation in human fetal hemoglobin in the infant and in certain hematological conditions in the adult. Proceedings of the XVII Colloquium, Protides of the BiologicalFluids; Bruges, Belgium. Pergamon Press, New York, NY, USA 1970; 249–255
   Google Scholar
• Schroeder W. A., Huisman T. H.J. Multiple cistrons for fetal hemoglobin in man. Ann. N.Y. Acad. Sci. 1974; 241: 70–79
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Harris H., Gravely M., Schroeder W. A., Shelton J. R., Shelton J. B., Evans L. The chemical heterogeneity of the fetal hemoglobin in normalnewborn infants and adults. Mol. Cell. Biochem. 1977; 17: 45–55
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. The polymorphism of human fetal hemoglobin. Thalassemia: Recent Advances in Detection and Treatment, A. Cao, U. Carcassi, P. T. Rowley, 1982; 18: 83–89
   Google Scholar
• Huisman T. H.J., Schroeder W. A., Keeling M. E., Gongozian N., Miller A., Brodie A. R., Shelton J. R., Shelton J. B., Apell G. Search for nonallelic structural genes of γ-chains offetal hemoglobin in some primates. Biochem. Genet. 1973; 10: 309–318
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Shelton J. R., Shelton J. B., Huisman T. H.J. The Vγ chain of fetal hemoglobin in the orangutan. Biochem. Genet. 1978; 16: 1203–1205
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Huisman T. H.J., Brown A. K., Uy R., Bouver N. G., Lerch P. O., Shelton J. R., Shelton J. B., Apell G. Postnatal changes in the chemical heterogeneity of human fetalhemoglobin. Pediatr. Res. 1971; 5: 493–499
   Web of Science ®Google Scholar
• Schroeder W. A., Shelton J. R., Shelton J. B., Apell G., Huisman T. H.J., Bouver N. G. World-wide occurrence of nonallelic genes for the γ-chainof human foetal haemoglobin in newborns. Nature New Biol. 1972; 240: 273–274
   PubMedGoogle Scholar
• Schroeder W. A., Bannister W. H., Grech J. L., Brown A. K., Wrightstone R. N., Huisman T. H.J. Non-synchronized suppression of postnatal activity in non-allelicgenes which synthesize the Gγ chain in human foetal haemoglobin. Nature New Biol. 1973; 244: 89–90
   PubMedGoogle Scholar
• Huisman T. H.J., Schroeder W. A., Felice A., Powars D., Ringelhann B. An anomaly of the γ chain heterogeneity of the newborn 1977; 265: 63–65
   Google Scholar
• Nakatsuji T., Carver J., Wilson J. B., Reese A. L., Nagle S., Huisman T. H.J. Alpha chain and gamma chain abnormal hemoglobins in newbornbabies: structural and genetic aspects. Am. J. Hematol 1983; 14: 121–132
   PubMed Web of Science ®Google Scholar
• Sukumaran P. K., Nakatsuji T., Gardiner M. B., Reese A. L., Gilman J. G., Huisman T. H.J. Gamma thalassemia resulting from the deletion of a γ-globingene. Nucleic Acids Res. 1983; 11: 4635–4643
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Fei Y. J., Kutlar F. (1988) Variations in Gγ and Aγratios in the fetal hemoglobin of newborn babies. Proceedings of the First International Symposium on Thalassemiasin China, ShanghaiPeople'sRepublic of China, October, 12–151987. 12 (5&6): 699–705, Hemoglobin
   Google Scholar
• Powers P. A., Altay C., Huisman T. H.J., Smithies O. Two novel arrangements of the human fetal globin genes: Gγ-Gγand Aγ-Aγ. Nucleic Acids Res. 1984; 12: 7023–7034
   PubMed Web of Science ®Google Scholar
• Harano T., Huisman T. H.J., Zeng Y. T., Huang S. Z. Two arrangements of the human fetal genes are responsible forhigh Gg values in Chinese newborns: -Gγ-Gγ- γ-β and-Gγ-AγGγ-Gγ-δ-β. Am. J. Hematol 1985; 19: 349–353
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Harano T., Nakatsuji T., Bakioglu I., Reese A. L., Gardiner M. B., Huisman T. H.J. The ratio of the Gγ and Aγ Chain: variations due to anomalies at the molecular level. Fifth Cooley's Anemia Symposium, A. Bank, W. F. Anderson, E. C. Zaino. Ann. N.Y. Acad. Sci. 1985; 445: 235–247
   Google Scholar
• Chu Z. F., Liang C. C., Kutlar F., Huisman T. H.J. Fetal hemoglobin heterogeneity in Chinese newborns of the Uygurand Han nationalities; comparisons of babies from Xinjiang and Beijing. Hemoglobin 1987; 11(2)123–128
   PubMed Web of Science ®Google Scholar
• Zeng Y-T., Huang S-Z., Chen B., Liang Y-C., Cham Z-M., Harano T., Huisman T. H.J. Hereditary persistence of fetal hemoglobin or (δβ)0-thalassemia:three types observed in South-Chinese families. Blood 1985; 66: 1430–1435
   PubMed Web of Science ®Google Scholar
• Harano T., Harano K., Ukita M., Wada Y., Hayashi A., Ohba Y., Miyaji T., Kutlar F., Huisman T. H.J. (1988) Characterization of abnormalities in the γ-globingene arrangements of Japanese newborns. Proceedingsof the First International Symposium on Thalassemias in China, ShanghaiPeople's Republic of China, October, 12–151987. 12 (5&6): 699–705, Haemoglobin
   Google Scholar
• Hattori Y., Kutlar F., Chen S. S., Huisman T. H.J., Demuro P., Formato M., Manca L., Masala B. DNA polymorphisms in North Sardinian newborns and their linkagewith abnormal γ globin gene arrangements and with b0-thalassemia. Biochem. Genet. 1986; 24: 669–681
   PubMed Web of Science ®Google Scholar
• Manca L., Masala B., Orzalezi M., Huang H. J., Huisman T. H.J. (1988) Abnormal g-globin gene arrangementsin Sardinians. Proceedings ofthe First International Symposium on Thalassemias in China, ShanghaiPeople's Republic of China, October, 12–151987. 12 (5&6): 741–753, Hemoglobin
   Google Scholar
• Fei Y. J., Kutlar F., Harris H. F., II, Wilson M. M., Milana A., Sciacca P., Schiliro G., Masala B., Manca L., Altay Ç, Gurgey A., de Pablos J. Ma., Villegas A., Huisman T. H.J. A search for anomalies in the ζ, α, β, and γglobin gene arrangements in normal black, Italian, Turkish, and Spanish newborns. Hemoglobin 1989; 13(1)45–65
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Reese A. L., Gardiner M. B., Wilson J. B., Lam H., Reynolds A., Nagle S., Trowell P., Zeng Y. T., Huang S. Z., Sukumaran P. K., Miwa S., Efremov G. D., Petkov G., Sciarratta G. V., Sansone G. The occurrence of different levels of Gγ and of the AγTTvariant of fetal hemoglobin in newborn babies from several countries. Am. J. Hematol 1983; 14: 133–148
   PubMed Web of Science ®Google Scholar
• Harano K., Harano T., Kutlar F., Huisman T. H.J. γ-Globin gene triplication and quadruplication in Japanesenewborns. Evidence for a decreased in vivo expression of the 3′-Aγ-globingene. FEBS Lett. 1985; 190: 45–49
   PubMed Web of Science ®Google Scholar
• Yang K. G., Liu J. Z., Kutlar F., Altay Ç, Gurgey A., Huisman T. H.J. β0-Thalassemia in association with γ globin genequadruplication. Blood 1986; 68: 1394–1397
   PubMed Web of Science ®Google Scholar
• Fei Y. J., Lanclos Ke D., Kutlar F., Walker E. L., III, Huisman T. H.J. A chromosome with five γ globin genes. Blood 1988; 72: 827–829
   PubMed Web of Science ®Google Scholar
• Altay C., Huisman T. H.J., Schroeder W. A. Another form of hereditary persistence of fetal hemoglobin (theAtlanta type). Hemoglobin 1977; 1(2)125–133
   Web of Science ®Google Scholar
• Harano T., Huisman T. H.J. Hemoglobin abnormalities in a black family with Hb S, hereditarypersistence of Hb F, and a γ chain variant; a reevaluation through genemapping. Hemoglobin 1984; 8(6)549–568
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Chen S. S., Nakatsuji T., Kutlar F. A second family with the Atlanta type of HPFH. Hemoglobin 1985; 9(4)393–398
   PubMed Web of Science ®Google Scholar
• Efremov D. G., Dimovski A. J., Huisman T. H.J. The –158 (C→T) promoter mutation is responsible forthe increased transcription of the 3′ γ gene in the Atlanta typeof hereditary persistence of fetal hemoglobin. Blood 1994; 83: 3350–3355
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Huisman T. H.J. Two independent genetic factors in the β-globin gene clusterare associated with high Gγ levels in the Hb F of SS patients. Blood 1984; 64: 452–457
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Huisman T. H.J. DNA sequence variation associated with elevated fetal Gγglobin production. Blood 1985; 66: 783–787
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Huisman T. H.J. A mutation associated with elevated Gγ chain in sickle cell anemia and hereditary persistence of fetal hemoglobin. Progress in Clinical and Biological Research, Experimental Approachesfor the Study of Hemoglobin Switching, G. Stamatoyannopoulos, A. W. Nienhuis. AlanR.Liss, Inc., New York, NY, USA 1985; 191: 141–149
   Google Scholar
• Gilman J. G., Kutlar F., Johnson M. E., Huisman T. H.J. A G to A nucleotide substitution 161 base pairs 5′ to the Gγ globin gene cap site (–161) in a high Gγ non-anemic person. Progress in Clinical and Biological Research, Developmental Controlof Globin Gene Expression, G. Stamatoyannopoulos, A. W. Nienhuis. Alan R. Liss, Inc., New York, NY, USA 1987; 251: 383–390
   Google Scholar
• Lanclos K. D., Michael S. K., Gu Y. C., Howard E. F., Stoming T. A., Huisman T. H.J. Transient chloramphenicol acetyltransferase expression of theGγ globin gene 5′-flanking regions containing substitutions ofC→T at position 7–158, G→A at position –161, and T→Aat position –175 in K562 cells. Biochim. Biophys. Acta 1989; 1008: 109–112
   PubMed Web of Science ®Google Scholar
• Liu J. Z., Gilman J. G., Cao Q., Bakioglu I., Huisman T. H.J. Four categories of γ-globin gene triplications: DNA sequencecomparison of low Gγ and high Gγ triplications. Blood 1988; 72: 480–484
   PubMed Web of Science ®Google Scholar
• Mitchener J. W., Thompson R. B., Huisman T. H.J. Foetal haemoglobin synthesis in some haemoglobinopathies. The Lancet 1961; I: 1169
   Google Scholar
• Huisman T. H.J., Schroeder W. A., Bouver N. G., Miller A., Shelton J. R., Shelton J. B., Apell G. Chemical heterogeneity of fetal hemoglobin in subjects withsickle cell anemia, homozygous Hb-C disease, SC-disease, and various combinationsof hemoglobin variants. Clin. Chim. Acta 1972; 38: 6–16
   Web of Science ®Google Scholar
• Wrightstone R. N., Huisman T. H.J. On the levels of hemoglobins F and A2 in sickle-cell anemiaand some related disorders. Am. J. Clin. Pathol 1974; 61: 375–381
   PubMed Web of Science ®Google Scholar
• Gardiner M. B., Reese A. L., Headlee M. E., Huisman T. H.J. The heterogeneity of the γ-chain of fetal hemoglobin inHb S heterozygotes. Blood 1982; 60: 513–518
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Reese A. L., Webber B., Okonjo K., Altay C., Felice A. E. In vitro synthesis of hemoglobin and hemoglobin chains in theBFUe-derived colonies from persons with α- or with β-thalassemia. Am. J. Hematol 1981; 10: 227–237
   PubMed Web of Science ®Google Scholar
• Miller B. A., Olivieri N., Salameh M., Ahmed M., Antognetti G., Huisman T. H.J., Nathan D. G., Orkin S. H. Molecular analysis of the highhemoglobin F phenotype in SaudiArabian sickle cell anemia. N. Engl. J. Med. 1987; 316: 244–250
   PubMed Web of Science ®Google Scholar
• Miller B. A., Salameh M., Ahmed M., Olivieri N., Huisman T. H.J., Orkin S. H., Nathan D. G. Analysis of high fetal hemoglobin production in sickle cell anemia patients from the Eastern Province of Saudi Arabia. Progress in Clinical and Biological Research, Developmental Controlof Globin Gene Expression, G. Stamatoyannopoulos, A. W. Nienhuis. Alan R. Liss, Inc., New York, NY, USA 1987; 251: 415–426
   Google Scholar
• Gilman J. G., Mishima N., Wen X. J., Johnson M. E., Kutlar F., Huisman T. H.J. Upstream promoter mutation associated with a modest elevationin fetal hemoglobin expression in human adults. Blood 1988; 72: 78–81
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Hereditary persistence of foetal haemoglobin in adult life. Proceedings of the Haemoglobin-Colloquium, ViennaAustria. H. Lehmann, K. Betke. Georg Thieme Verlag, StuttgartGermany 1961; 77–82
   Google Scholar
• Huisman T. H.J., Schroeder W. A., Dozy A. M., Shelton J. R., Shelton J. B., Boyd E. M., Apell G. Evidence for multiple structural genes for the gammachain ofhuman fetal hemoglobin in hereditary persistence of fetal hemoglobin. Ann. N.Y. Acad. Sci. 1969; 165: 320–331
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Schroeder W. A., Charache S., Bethlenfalvay N. C., Bouver N., Shelton J. R., Shelton J. B., Apell G. Hereditary persistence of fetal hemoglobin. Heterogeneity offetal hemoglobin in homozygotes and in conjunction with β-thalassemia. N. Engl. J. Med. 1971; 285: 711–716
   PubMed Web of Science ®Google Scholar
• Forget B. G., Hillman D. G., Lazarus H., Barell E. F., Benz E. J., jr., Caskey C. T., Huisman T. H.J., Schroeder W. A., Housman D. Absence of messenger RNA and gene DNA for β-globin chainsin hereditary persistence of fetal hemoglobin. Cell 1976; 7: 323–329
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Gravely M. E., Sox R. A note on the inheritance of the hereditary persistence of fetalhaemoglobin and the δ-chain variant Hb A′2. J. Med. Genet 1976; 13: 62–63
   PubMed Web of Science ®Google Scholar
• McRoyan D. K., Liu P. I., Mancad V. N., Wilson J. B., Huisman T. H.J. Hb A2-Babinga, Hb S, and HPFH in members of a black family fromCreola, Alabama. Hemoglobin 1984; 8(4)413–416
   PubMed Web of Science ®Google Scholar
• Ringelhann B., Acquaye C. T.A., Oldham J. H., Konotey-Ahulu F. I.D., Yawson G., Sukumaran P. K., Schroeder W. A., Huisman T. H.J. Homozygotes for the hereditary persistence of fetal hemoglobin:the ratio of Gγ to Aγ Chain and biosynthetic studies. Biochem. Genet. 1977; 15: 1083–1096
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. The first homozygote for the hereditary persistence of fetalhemoglobin observed in the Southeastern United States. Hemoglobin 1981; 5(4)411–416
   PubMed Web of Science ®Google Scholar
• Schroseder W. A., Huisman T. H.J., Sukumaran P. K. A second type of hereditary persistence of foetal haemoglobinin India. Br. J. Haematol 1973; 25: 131–135
   PubMed Web of Science ®Google Scholar
• Henthorn P. S., Mager D. L., Huisman T. H.J., Smithies O. A gene deletion ending within a complex array of repeated sequences3′ to the human β-globin gene cluster. Proc. Natl. Acad. Sci. USA 1986; 83: 5194–5198
   PubMed Web of Science ®Google Scholar
• Kutlar A., Gardiner M. B., Headlee M. G., Reese A. L., Cleek M. P., Nagle S., Sukumaran P. K., Huisman T. H.J. Heterogeneity in the molecular basis of three types of hereditarypersistence of fetal hemoglobin and the relative synthesis of the Gγand Aγ types of γ chain. Biochem. Genet. 1984; 22: 21–35
   PubMed Web of Science ®Google Scholar
• Boyer S. H., Margolet L., Boyer M. L., Huisman T. H.J., Schroeder W. A., Wood W. G., Weatherall D. J., Clegg J. B., Cartner R. Inheritance of F cell frequency in heterocellular hereditarypersistence of fetal hemoglobin: an example allelic exclusion. Am. J. Hum. Genet. 1977; 29: 256–271
   PubMed Web of Science ®Google Scholar
• Yang K. G., Stoming T. A., Fei Y. J., Liang S., Wong S. C., Masala B., Huang R. B., Wei Z. P., Huisman T. H.J. Identification of base substitutions in the promoter regionsof the Aγ- and Gγ-globin genes in Aγ- (or Gγ-) β+-HPFHheterozygotes using the DNA-amplification-synthetic oligonucleotide procedure. Blood 1988; 71: 1414–1417
   PubMed Web of Science ®Google Scholar
• Huang H. J., Stoming T. A., Harris H. F., Kutlar F., Huisman T. H.J. The Greek Aγβ+-HPFH observed in a large black family. Am. J. Hematol. 1987; 25: 401–408
   PubMed Web of Science ®Google Scholar
• Stoming T. A., Stoming G. S., Lanclos K. D., Fei Y. J., Altay Ç, Kutlar F., Huisman T. H.J. An Aγ type of nondeletional hereditary persistence offetal hemoglobin with a T→C mutation at position ndash;175 to the capsite of the Aγ globin gene. Blood 1989; 73: 329–333
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Mishima N., Wen X. J., Stoming T. A., Lobel J., Huisman T. H.J. Distal CCAAT box deletion in the Aγ globin gene of twoblacks with elevated fetal Aγ globin. Nucleic Acids Res. 1988; 16: 10635–10642
   PubMed Web of Science ®Google Scholar
• Stamatoyannopoulos G., Schroeder W. A., Huisman T. H.J., Shelton J. R., Shelton J. B., Apell G., Bouver N. Nature of foetal haemoglobin in F-thalassaemia. Br. J. Haematol 1971; 21: 633–642
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Nikolov N., Duma H., Schroeder W. A., Miller A., Huisman T. H.J. δβ-thalassaemia in two Yugoslavian families. Scand. J. Haematol 1975; 14: 226–232
   PubMedGoogle Scholar
• Efremov G. D., Filipce V., Gjorgovski I., Juricic D., Stojanovski N., Harano T., Nakatsuji T., Kutlar A., Kutlar F., Bakioglu I., Huisman T. H.J. GγAγ(δβ)0- thalassaemia and a new formof γ globin gene triplication identified in the Yugoslavian population. Br. J. Haematol 1986; 63: 17–28
   PubMed Web of Science ®Google Scholar
• Ruiz-Reyes G., Pina-Camara A., Felice A. E., Gravely M. E., Huisman T. H.J. δβ-thalassemia in a Mexican family. Hemoglobin 1978; 2(6)513–529
   PubMed Web of Science ®Google Scholar
• Dincol G., Altay C., Aksoy M., Gurgey A., Felice A. E., Huisman T. H.J. Clinical and hematological evaluation of two δ0β0-thalassemiahomozygotes. Hemoglobin 1981; 5(2)153–164
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Nikolov N., Bakioglu I., Huisman T. H.J. The 18 to 23 kb deletion of the Macedonian δβ thalassemiaIncludes the entire δ and β globin genes. Blood 1986; 68: 971–974
   PubMed Web of Science ®Google Scholar
• Altay C., Schroeder W. A., Huisman T. H.J. The Gγ-δβ-thalassemia and Gγ-β0-HPFH conditions in combination with β-thalassemia and Hb S. Am. J. Hematol 1977; 3: 1–14
   PubMed Web of Science ®Google Scholar
• Sukumaran P. K., Huisman T. H.J., Schroeder W. A., McCurdy P. R., Freehafer J. T., Bouver N., Shelton J. R., Shelton J. B., Apell G. A homozygote for the HbGγ type of foetal haemoglobin inIndia: a study of two Indian and four Negro families. Br. J. Haematol 1972; 23: 403–417
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Gilman J. G., Sukumaran P. K., Huisman T. H.J. Restriction endonuclease gene mapping studies of an Indian (Aγδβ)0-thalassaemiapreviously identified as Gγ-HPFH. Br. J. Haematol 1984; 57: 663–670
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Wilson J. B. The use of HPLC procedures in the study of human hemoglobin variants. Proceedings of the XXXII Colloquium, Protides of the BiologicalFluids, H. Peters, BrusselsBelgium 1984; 1029–1036
   Google Scholar
• George E., Faridah K., Trent R. J., Padanilam B. J., Huang H-J., Huisman T. H.J. Homozygosity for a new type of Gγ(Aγδβ)0-thalassemiain a Malaysian male. Hemoglobin 1986; 10(4)353–363
   PubMed Web of Science ®Google Scholar
• Henthorn P. S., Smithies O., Nakatsuji T., Felice A. E., Gardiner M. B., Reese A. L., Huisman T. H.J. (Aγδβ)0-thalassaemia in blacks is due to adeletion of 34 kpb of DNA. Br. J. Haematol 1985; 59: 343–356
   PubMed Web of Science ®Google Scholar
• Diaz-Chico J. C., Huang H. J., Juricic D., Efremov G. D., Wadsworth L. D., Huisman T. H.J. Two new large deletions resulting in εγδβ-thalassemia. Acta Haematol 1988; 80: 79–84
   PubMed Web of Science ®Google Scholar
• Abels J., Michiels J. J., Giordano P. C., Bernini L. F., Baysal E., Smetanina N. S., Kazanetz E. G., Leonova J. Ye., Huisman T. H.J. A de novo deletion causing εγδβ-thalassemiain a Dutch patient. Hemoglobin 1996; 20(2)131–134
   PubMedGoogle Scholar
• Huisman T. H.J., Schroeder W. A., Efremov G. D., Duma H., Mladenovski B., Hyman C. B., Rachmilewitz E. A., Bouver N., Miller A., Brodie A., Shelton J. R., Shelton J. B., Apell G. The present status of the heterogeneity of fetal hemoglobinin β-thalassemia: an attempt to unify some observations in thalassemiaand related conditions. Ann. N.Y. Acad. Sci. 1974; 232: 107–124
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Kutlar F., Gu L-H. γ Chain abnormalities and γ-globin gene rearrangementsin newborn babies of various populations. Hemoglobin 1991; 15(5)349–379
   PubMed Web of Science ®Google Scholar
• Dimovski A. J., Adekile A. D., Huisman T. H.J. The in vivo expression of the globin genes of the β cistronin γ-, δ-, and δβ-thalassemia. Experientia 1994; 50: 167–170
   PubMedGoogle Scholar
• Abraham E. C., Walker D., Gravely M., Huisman T. H.J. Minor hemoglobins in sickle cell anemia, β-thalassemia,and related conditions: a study of red cell fractions isolated by densitygradient centrifugation. Biochem. Med. 1975; 13: 56–77
   PubMedGoogle Scholar
• Abraham E. C., Stallings M., Cameron B. F., Huisman T. H.J. Minor hemoglobin in sickle-cell heterozygotes and homozygoteswith and without diabetes. Biochim. Biophys. Acta 1980; 625: 109–117
   PubMedGoogle Scholar
• Headlee M. E., Gardiner M. B., Reese A. L., Huisman T. H.J. The distribution of fetal hemoglobin and the types of γchain in red cell fractions separated by gradient centrifugation. Biochem. Med. 1983; 29: 337–354
   PubMed Web of Science ®Google Scholar
• Reese A. L., Altay C., Headlee M. E., Gardiner M. B., Webber B., Jonah F., Wilson J. B., Huisman T. H.J. The percentages of Hb F and of Gγ and Aγ Chain inthe Hb F synthesized by reticulocytes and BFUe-derived colonies of patientswith sickle cell anemia. Hemoglobin 1982; 6(4)369–378
   PubMed Web of Science ®Google Scholar
• Bhaumik K., Huisman T. H.J. Application of high performance liquid chromatographic methodologyto the analysis of hemoglobins synthesized in erythroid progenitor cells. J. Chromatogr. 1989; 496: 83–89
   PubMed Web of Science ®Google Scholar
• Kumpati J., Huisman T. H.J., Efremov G. D. Interaction between human hemoglobin variants and hemoglobinS. Proc. Soc. Exp. Biol. Med. 1978; 157: 250–252
   PubMed Web of Science ®Google Scholar
• Abraham E. C., Carver J., Döbler J., Milner P. F., Huisman T. H.J. Microchromatographic quantitation of fetal hemoglobin in patientswith sickle cell disease. Hemoglobin 1979; 3(5)341–351
   PubMed Web of Science ®Google Scholar
• Hattori Y., Kutlar F., Kutlar A., McKie V. C., Huisman T. H.J. Haplotypes of βS chromosomes among patients with sicklecell anemia from georgia. Hemoglobin 1986; 10(6)623–642
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M., Nechtman C., Thompson R. B. Oxygen equilibrium of haemoglobin A2 and its variant haemoglobinA′2(or B2). Nature 1962; 195: 1109–1110
   PubMed Web of Science ®Google Scholar
• Wrightstone R. N., Huisman T. H.J., van der Sar A. Qualitative and quantitative studies of sickle cell hemoglobinin homozygotes and heterozygotes. Clin. Chim. Acta 1967; 22: 593–601
   Web of Science ®Google Scholar
• Aluoch J. R., Kilinç Y., Aksoy M., Yuregir G. T., Bakioglu I., Kutlar A., Kutlar F., Huisman T. H.J. Sickle cell anaemia among Eti-Turks; haematological, clinicaland genetic observations. Br. J. Haematol 1986; 64: 45–55
   PubMed Web of Science ®Google Scholar
• Yüregir G. T., Aksoy K., Çürük M. A., Taeih I. M., Zhao W., Huisman T. H.J. Sickle cell anemia and thalassemia in Lattakia, Syria. Doga-Tr. J. Med. Sci. 1992; 16: 183–185
   Google Scholar
• Kutlar A., Hattori Y., Bakioglu I., Kutlar F., Kamel K., Huisman T. H.J. Hematological observations on Arabian SS patients with a homozygosityor heterozygosity for a βS chromosome with haplotype #31. Hemoglobin 1985; 9(6)545–557
   PubMed Web of Science ®Google Scholar
• Miller B. A., Salameh M., Ahmed M., Olivieri N., Antognetti G., Orkin S., Huisman T. H.J., Nathan D. G. Analysis of hemoglobin F production in Saudi Arabian familieswith sickle cell anemia. Blood 1987; 70: 716–720
   PubMed Web of Science ®Google Scholar
• Miller B. A., Salameh M., Ahmed M., Olivieri N., Huisman T. H.J., Orkin S. H., Nathan D. G. Saudi Arabian sickle cell anemia. A Molecular Approach. Ann. N.Y. Acad. Sci. 1989; 565: 143–151
   PubMed Web of Science ®Google Scholar
• Adekile A. D., McKie K. M., Adeodu O. O., Sulzer A. J., McKie V. C., Kutlar F., Ramachandran M., Kaine W., Akenzua G. I., Akolo A. A., Asindi A. A., Obinyan E. A., Ogala W. N., Ibrahim M., Huisman T. H.J. The spleen in sickle cell anemia: comparative studies of Nigerianand U.S. patients. Am. J. Hematol 1993; 42: 316–321
   PubMed Web of Science ®Google Scholar
• Saleh A. W., Jr., van Goethem A., Jansen R., Velvis H. J.R., Gu L-H., Huisman T. H.J. Isobutyramide therapy in patients with sickle cell anemia. Am. J. Hematol 1995; 49: 244–246
   PubMed Web of Science ®Google Scholar
• Saleh A. W., Jr., Velvis H. J.R., Gu L-H., Hillen H. F.P., Huisman T. H.J. Hydroxyurea therapy in sickle cell anemia patients in Curaçao,the Netherlands Antilles. Acta Haematol 1997; 98: 125–129
   PubMed Web of Science ®Google Scholar
• Kutlar F., Fei Y. J., Wilson J. B., Kutlar A., Huisman T. H.J. Detection of the embryonic ζ chain in blood from newbornbabies by reversed-phase high-performance liquid chromatography. J. Chromatogr. 1987; 394: 333–343
   PubMed Web of Science ®Google Scholar
• Fuhr J. E., Bamberger E., Lozzio C. B., Lozzio B. B., Felice A. E., Altay G., Webber B. B., Reese A. L., Mayson S. M., Huisman T. H.J. Identification and quantitation of embryonic and three typesof fetal hemoglobin produced on induction of the human pluripotent leukemiacell line K-562 with hemin. Am. J. Hematol. 1982; 12: 1–12
   PubMed Web of Science ®Google Scholar
• Kutlar F., Moscoso H., Kiefer C. R., Garver F. A., Beksaç S., Önderoglu L., Gurgey A., Altay Ç, Huisman T. H.J. The quantities of adult, fetal, and embryonic globin chainsin the blood of eighteen to twenty-week-old fetuses. J. Chromatogr. 1991; 567: 359–368
   PubMed Web of Science ®Google Scholar
• Kutlar F., Gu L. H., Hu H., Huisman T. H.J. Quantitation of hemoglobins Bart's, H, Portland-I, Portland-IIand constant spring by anion-exchange high-performance liquid chromatography. J. Chromatogr. 1989; 487: 265–274
   PubMed Web of Science ®Google Scholar
• Baysal E., Huisman T. H.J. Detection of common deletional α-thalassemia-2 determinantsby PCR. Am. J. Hematol. 1994; 46: 208–213
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Huisman T. H.J. Detection of α-thalassemia-2 (–3.7 kb) and its correspondingtriplication ααα (anti 3.7 kb) by PCR; an improved technicalchange. Am. J. Hematol. 1996; 53: 202–203
   PubMed Web of Science ®Google Scholar
• Okeagu J. E., Smetanina N. S., Huisman T. H.J. Detection of the α-thalassemia-2 (3.7 kb) deletion inDNA extracted from 20–year-old blood smears. Hemoglobin 1997; 21(1)53–58
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Genetic aspects of two different minor haemoglobin componentsfound in cord blood samples of Negro babies. Nature 1960; 188: 589–590
   PubMed Web of Science ®Google Scholar
• Horton B. F., Thompson R. B., Dozy A. M., Nechtman C. M., Nichols E., Huisman T. H.J. Inhomogeneity of hemoglobin. VI. the ninor hemoglobin componentsof cord blood. Blood 1962; 20: 302–314
   PubMed Web of Science ®Google Scholar
• Altay C., Ringelhann B., Yawson G. I., Bruce-Tagoe A. A., Konotey-Ahulu F. I.D., James L., Gravely M., Huisman T. H.J. Hemoglobin a chain deficiency in black children with variablequantities of hemoglobin Bart's at birth. Pediatr. Res. 1977; 2: 147–152
   Google Scholar
• Huisman T. H.J. Trimodality in the percentages of α chain variants inheterozygotes: the effect of the number of active Hbα structural loci. Hemoglobin 1977; 1(4)349–382
   PubMed Web of Science ®Google Scholar
• Felice A., Abraham E. C., Miller A., Cope N., Gravely M., Huisman T. H.J. Posttranslational control of human hemoglobin synthesis: the number of α chain genes in the synthesis of Hb S. The Red Cell, R. Alan. Liss Inc., New York, NY, USA 1978; 131–154
   Google Scholar
• Henson J., Huisman T. H.J. Possible relationship between the level of Hb Bart's (γ4)and the relative amount of Hb S or Hb C in black heterozygous newborn. Hemoglobin 1978; 2(4)393–398
   PubMed Web of Science ®Google Scholar
• Felice A. E., Webber B., Miller A., Mayson S. M., Harris H. F., Henson J. B., Gravely M. E., Huisman T. H.J. The association of sickle cell anemia with heterozygous andhomozygous α-thalassemia-2: in vitro Hb chain synthesis. Am. J. Hematol. 1979; 6: 91–106
   PubMed Web of Science ®Google Scholar
• Felice A. E., Webber B. B., Huisman T. H.J. α-Thalassemia and the production of different a chainvariants in heterozygotes. Biochem. Genet. 1981; 19: 487–498
   PubMed Web of Science ®Google Scholar
• Felice A. E., Altay C. A., Milner P. F., Huisman T. H.J. The occurrence and identification of α-thalassemia-2 amongHb S heterozygotes. Am. J. Clin. Pathol. 1981; 76: 70–73
   PubMed Web of Science ®Google Scholar
• Baysal E., Qin W-B., Huisman T. H.J. α-Thalassemia and fetal hemoglobin. Blood 1994; 84: 3241–3242
   PubMed Web of Science ®Google Scholar
• Daenen S., Reese A. L., Kutlar F., Huisman T. H.J. An Indonesian family with the Southeast Asian type of α-thalassaemia-1and a γ globin gene triplication. Acta Haematol. 1987; 78: 23–27
   PubMed Web of Science ®Google Scholar
• Zhao J-B., Zhao L., Gu Y-C., Huisman T. H.J. Types of α-globin gene deficiencies in Chinese newbornbabies in the Guangxi Region, P.R. China. Hemoglobin 1992; 16(4)325–328
   PubMed Web of Science ®Google Scholar
• Fei Y-J., Liu J-C., Jogessar V. B., Westermeyer K. R., Bridgemohan R., Huisman T. H.J. Combination of three different forms of α-thalassemiain a large Indian family from Durban, South Africa; hematological observations. Acta Haematol 1992; 87: 11–15
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Wrightstone R. N., Huisman T. H.J., Schroeder W. A., Hyman C., Ortega J., Williams K. An unusual hemoglobin anomaly and its relation to α-thalassemiaand hemoglobin-H disease. J. Clin. Invest. 1971; 50: 1628–1636
   PubMed Web of Science ®Google Scholar
• Zeng Y. T., Huang S. Z., Zhou X. D., Sheng M., Feng J. P., Chen M. J., Qiu X. K., Yu S. C., Wang C. Q., Zhou X. M., Tang L. P., Lam H., Wilson J. B., Huisman T. H.J. A study of one family with hemoglobin Q-Thailand (α2 74(EF3)Asp→His β2) found in China. Acta Biochem. Biophys. Sin. 1983; 15: 423
   Google Scholar
• Beris P., Huber P., Miescher P. A., Wilson J. B., Kutlar A., Chen S. S., Huisman T. H.J. Hb Q-Thailand-Hb H disease in a Chinese living in Geneva, Switzerland:characterization of the variant and identification of two α-thalassemicchromosomes. Am. J. Hematol 1987; 24: 395–400
   PubMed Web of Science ®Google Scholar
• Felice A. E., Cleek M. P., McKie K., McKie V., Huisman T. H.J. The rare α-thalassemia-1 of blacks is a ζα-thalassemia-1associated with deletion of all α- and ζ-globin genes. Blood 1984; 63: 1253–1257
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Josifovska O., Nikolov N., Codrington J. F., Oner C., Gonzalez-Redondo J. M., Huisman T. H.J. Hb Icaria-Hb H disease; identification of the Hb Icaria mutationthrough analysis of amplified DNA. Br. J. Haematol 1990; 75: 250–253
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Diaz-Chico J. C., Malcorra-Azpiazu J. J., Balda-Aguirre M. I., Huisman T. H.J. Characterization of a newly discovered α-thalassaemia-1in two Spanish patients with Hb H disease. Br. J. Haematol 1988; 70: 459–463
   PubMed Web of Science ®Google Scholar
• Baysal E., Kleanthous M., Bozkurt G., Kyrri A., Kalogirou E., Angastiniotis M., Ioannou P., Huisman T. H.J. α-Thalassaemia in the population of Cyprus. Br. J. Haematol 1995; 89: 496–499
   PubMed Web of Science ®Google Scholar
• Yuregir G. T., Aksoy K., Çuruk M. A., Dikmen N., Fei Y-J., Baysal E., Huisman T. H.J. Hb H Disease in a Turkish family resulting from the interactionof a deletional α-thalassaemia-1 and newly discovered poly A mutation. Br. J. Haematol 1992; 80: 527–532
   PubMed Web of Science ®Google Scholar
• Çürük M. A., Dimovski A. J., Baysal E., Gu L-H., Kutlar F., Molchanova T. P., Webber B. B., Altay Ç, Gurgey A., Huisman T. H.J. Hb Adana or α259(E8) Gly→Aspβ2, a severely unstableα1–globin variant, observed in combination with the -(α)20.5kb α-Thal-1 deletion in two Turkish patients. Am. J. Hematol 1993; 44: 170–175
   Google Scholar
• Adekile A. D., Gu L-H., Baysal E., Haider M. Z., al-Fuzae L., Aboobacker K. C., Al-Rashied A., Huisman T. H.J. Molecular characterization of α-thalassemia determinants,β-thalassemia alleles, and βS haplotypes among Kuwaiti arabs. Acta Haematol 1994; 92: 176–181
   PubMed Web of Science ®Google Scholar
• Gu Y-C., Nakatsuji T., Huisman T. H.J. Detection of a new hybrid α2 globin gene among americanblacks. Hum. Genet. 1988; 79: 68–72
   PubMed Web of Science ®Google Scholar
• Nakatsuji T., Landman H., Huisman T. H.J. An elongated segment of DNA observed between two human αglobin genes. Hum. Genet. 1986; 74: 368–371
   PubMed Web of Science ®Google Scholar
• Gu Y. C., Landman H., Huisman T. H.J. Two different quadruplicated a globin gene arrangements. Br. J. Haematol 1987; 66: 245–250
   PubMed Web of Science ®Google Scholar
• Fei Y. J., Fujita S., Huisman T. H.J. Two different theta (thetas) globin gene deletions observerdamong black newborn babies. Br. J. Haematol 1988; 68: 249–253
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Hans I-S., Gu Y-C., Huisman T. H.J. Nucleotide sequence of the human thetas1 globin gene. Biochem. Genet. 1988; 26: 207–211
   PubMed Web of Science ®Google Scholar
• Milner P. F., Huisman T. H.J. Studies on the proportion and synthesis of haemoglobin G Philadelphiain red cells of heterozygotes, a homozygote, and a heterozygote for both haemoglobinG and α thalassaemia. Br. J. Haematol 1976; 34: 207–220
   PubMed Web of Science ®Google Scholar
• Felice A. E., Mayson S. M., Webber B. B., Miller A., Gravely M. E., Huisman T. H.J. Hb S, Hb G-Philadelphia and α-thalassemia-2 in a blackfamily. Pediatr. Res. 1980; 14: 266–267
   PubMed Web of Science ®Google Scholar
• Felice A. E., Ozdonmez R., Headlee M. E., Huisman T. H.J. Organization of α-chain genes among Hb G-Philadelphiaheterozygotes in association with Hb S, β-thalassemia and α-thalassemia-2. Biochem. Genet. 1982; 20: 689–701
   PubMed Web of Science ®Google Scholar
• Kutlar F., Kutlar A., Nuguid E., Prchal J., Huisman T. H.J. Usefulness of HPLC methodology for the characterization of combinationsof the common β chain variants Hbs S, C, and O-Arab, and the αchain variant Hb G-Philadelphia. Hemoglobin 1993; 17(1)55–66
   PubMed Web of Science ®Google Scholar
• Zeng Y. T., Headlee M. E., Henson J., Lam H., Wilson J. B., Huisman T. H.J. Identification of hemoglobin G-Philadelphia (α68 Asn→Lys)and hemoglobin Matsue-Oki (α75 Asp→Asn) in a black infant. Biochim. Biophys. Acta 1982; 707: 206–212
   PubMed Web of Science ®Google Scholar
• Sciarratta G. V., Sansone G., Ivaldi G., Felice A. E., Huisman T. H.J. Alternate organization of α G-Philadelphia globin genesamong U.S. black and italian Caucasian heterozygotes. Hemoglobin 1984; 8(6)537–547
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Huisman T. H.J., Shelton J. R., Shelton J. B., Apell G., Bouver N. Heterogeneity of fetal hemoglobin in β-thalassemia of theNegro. Am. J. Hum. Genet. 1970; 22: 505–514
   PubMed Web of Science ®Google Scholar
• Rachmilewitz E. A., Huisman T. H.J., Schroeder W. A. Heterogeneity of fetal hemoglobin among Israeli families withβ-thalassemia. Israel J. Med. Sci. 1973; 9: 1464–1468
   PubMedGoogle Scholar
• Schroeder W. A., Huisman T. H.J., Shelton J. R., Apell G., Shelton J. B., Brodie A. R., Lutcher C. L., Blunt M. B., Miller A. On the structure of hemoglobins A, A2, and F in a Negro withhomozygous beta;-thalassemia. Biochem. Med. 1974; 10: 276–292
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Efremov G. D., Reese A. L., Howard J. S., Gravely M. E., Wilson J. B. The ratio of Gγ and Aγ chains of hemoglobin F synthesized by BFU-E-derived colonies from blood of subjects with β+ thalassemia and related hemoglobinopathies. Proceedings of the 4th International Symposium on Cooley'sAnemia, F. W. Anderson, A. Bank, E. C. Zaino, 1980; 344: 253–261, Ann. N.Y. Acad. Sci.
   Google Scholar
• Huisman T. H.J., Efremov G. D., Reese A. L., Howard J. S., Gravely M. E., Harris H. F., Wilson J. B. The synthesis of fetal hemoglobin types in red blood cells andin BFU-E derived colonies from peripheral blood of patients with sickle cellanemia, β+- and δβ-thalassemia, various forms of hereditarypersistence of fetal hemoglobin, normal adults and newborn. Hemoglobin 1979; 3(4)223–252
   PubMed Web of Science ®Google Scholar
• Schroeder W. A., Huisman T. H.J. Hemoglobin F in β thalassemia and related conditions. Proceedings of the 4th International Symposium on Cooley'sAnemia, F. W. Anderson, A. Bank, E. C. Zaino, 1980; 344: 240–252, Ann. N.Y. Acad. Sci.
   Google Scholar
• Huisman T. H.J., Reese A. L., Gravely M. E., Harris H., Wilson J. B. The synthesis of the Gγ and Aγ chains of fetal hemoglobinin erythroid colonies cultured from peripheral blood BFUe's of normaladults and newborn and of subjects with an Aγ or a Gγ chain abnormalfetal hemoglobin. Am. J. Hematol 1980; 9: 137–150
   PubMedGoogle Scholar
• Huisman T. H.J., Reese A. L., Gravely M. E., Wilson J. B., Webber B., Felice A. E. (1980) Abnormalities in Hemoglobinand Red Cell Enzymes, Section A: Hemoglobin and Its Abnormalities. Adult and fetal hemoglobin production in erythroid coloniesfrom subjects with β- thalassemia or with hereditary persistence of fetalhemoglobin (HPFH). Proceedingsof the U.S.–Japan Cooperative Science Program, Honolulu, HI, USA, January, 14–181980. 4 (3&4): 449–467, Hemoglobin
   Google Scholar
• Huisman T. H.J., Gravely M. E., Webber B., Okonjo K., Henson J., Reese A. L. The gamma chain heterogeneity of fetal hemoglobin in black β-thalassemiaand HPFH heterozygotes. Blood 1981; 58: 62–70
   PubMed Web of Science ®Google Scholar
• Harano T., Reese A. L., Ryan R., Abraham B. L., Huisman T. H.J. Five haplotypes in black β-thalassaemia heterozygotes:three are associated with high and two with low Gγ values in fetal haemoglobin. Br. J. Haematol 1985; 59: 333–342
   PubMed Web of Science ®Google Scholar
• Lee R. C., Huisman T. H.J. β Thalassemia-hemoglobin Dα a family report. Am. J. Hum. Genet. 1965; 17: 148–155
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Huisman T. H.J., Stojanovski N., Efremov G. D. Characterization of the β+-thalassemia mutation in a homozygousYugoslavian patient. Hemoglobin 1984; 8(5)529–534
   PubMed Web of Science ®Google Scholar
• Padanilam B. J., Huisman T. H.J. The β0-thalassemia in an American black family is due toa single nucleotide substitution in the acceptor splice junction of the secondintervening sequence. Am. J. Hematol 1986; 22: 259–263
   PubMed Web of Science ®Google Scholar
• Diaz-Chico J. C., Yang K-G., Yang K-Y., Efremov D. G., Stoming T. A., Huisman T. H.J. The detection of β-globin gene mutations in β-thalassemiausing nucleotide probes and amplified DNA. Biochim. Biophys. Acta 1988; 949: 43–48
   PubMed Web of Science ®Google Scholar
• Kutlar A., Kutlar F., Aksoy M., Gurgey A., Altay Ç, Wilson J. B., Diaz-Chico J. C., Hu H., Huisman T. H.J. β-Thalassemia intermedia in two Turkish families is causedby the interaction of Hb Knossos [β27(B9)Ala→Ser] and Hb city ofhope [β69(E13)Gly→Ser] with β0-thalassemia. Hemoglobin 1989; 13(1)7–16
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Stoming T. A., Kutlar F., Kutlar A., Hu H., Wilson J. B., Huisman T. H.J. Hb Monroe or α2β230(B12)Arg→Thr, a variant associatedwith β- thalassemia due to a G→C substitution adjacent to the donorsplice site of the first intron. Hemoglobin 1989; 13(1)67–74
   PubMed Web of Science ®Google Scholar
• Stoming T. A., Diaz-Chico J. C., Yang K. G., Efremov D. G., Huisman T. H.J. (1988) Newer developments in the identificationof β-thalassemia. Proceedingsof the First International Symposium on Thalassemias in China, ShanghaiPeople's Republic of China, October, 12–151987. 12 (5&6): 565–576, Hemoglobin
   Google Scholar
• Gonzalez-Redondo J. M., Stoming T. A., Kutlar A., Kutlar F., Lanclos K. D., Howard E. F., Fei Y. J., Aksoy M., Altay Ç, Gurgey A., Başak A. N., Efremov G. D., Petkov G., Huisman T. H.J. A C→T Substitution at nt –101 in a conserved DNAsequence of the promoter region of the β-globin gene is associated with“silent'” β-thalassemia. Blood 1989; 73: 1705–1711
   PubMed Web of Science ®Google Scholar
• Kollia P., Gonzalez-Redondo J. M., Stoming T. A., Loukopoulos D., Politis C., Huisman T. H.J. Frameshift codon 5 [FSC-5 (–CT)] thalassemia; a novelmutation detected in a Greek patient. Hemoglobin 1989; 13(6)597–604
   PubMed Web of Science ®Google Scholar
• Oner R., Agarwal S., Dimovski A. J., Efremov G. D., Petkov G. H., Altay Ç, Gurgey A., Huisman T. H.J. The G→A mutation at position 22 3′ to the cap siteof the β-globin gene as a possible cause for a β-thalassemia. Hemoglobin 1991; 15(1)67–76
   PubMed Web of Science ®Google Scholar
• Jankovic L., Dimovski A. J., Kollia P., Karageorga M., Loukopoulos D., Huisman T. H.J. A C→G Mutation at nt position 6 3′ to the terminatingcodon may be the cause of a silent β-thalassemia. Int. J. Hematol 1991; 54: 289–293
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Stoming T. A., Lanclos K. D., Gu Y. C., Kutlar A., Kutlar F., Nakatsuji T., Deng B., Han I. S., McKie V. C., Huisman T. H.J. Clinical and genetic heterogeneity in black patients with homozygousβ-thalassemia from the Southeastern United States. Blood 1988; 72: 1007–1014
   PubMed Web of Science ®Google Scholar
• Gonzalez-Redondo J. M., Stoming T. A., Kutlar F., Kutlar A., Huisman T. H.J. Clinical and molecular characterization of thalassemia intermediaand thalassemia major in American blacks. Ann. N.Y. Acad. Sci. 1989; 565: 298–401
   Web of Science ®Google Scholar
• Codrington J., Anijs J., Wisse J. H., Codrington F. A., Li H., Kutlar F., Ramachandran M., Huisman T. H.J. Compound heterozygosity for a mild β+- and rare β0-thalassemiaallele. Acta Haematol 1990; 84: 135–138
   PubMed Web of Science ®Google Scholar
• Diaz-Chico J. C., Yang K. G., Stoming T. a., Efremov D. G., Kutlar A., Kutlar F., Aksoy M., Altay Ç, Gurgey A., Kilinç Y., Huisman T. H.J. Mild and severe β-thalassemia among homozygotes from turkey:identification of the types by hybridization of amplified DNA with syntheticprobes. Blood 1988; 71: 248–251
   PubMed Web of Science ®Google Scholar
• Gurgey A., Altay Ç, Diaz-Chico J. C., Kutlar F., Kutlar A., Huisman T. H.J. Molecular heterogeneity of beta-thalassemia intermedia in Turkey. Acta Haematol 1989; 81: 22–27
   PubMed Web of Science ®Google Scholar
• Oner R., Altay Ç, Gurgey A., Aksoy M., Kilinç Y., Stoming T. A., Reese A. L., Kutlar A., Kutlar F., Huisman T. H.J. β-thalassemia in Turkey. Hemoglobin 1990; 14(1)1–13
   PubMed Web of Science ®Google Scholar
• Masala B., Manca L., Gallisai D., Stangoni A., Lanclos K. D., Diaz-Chico J. C., Yang K. G., Huisman T. H.J. (1988) Biochemical and molecular aspects of β-thalassemiatypes in Northern Sardinia. Proceedingsof the First International Symposium on Thalassemias in China, ShanghaiPeople's Republic of China, October, 12–151987. 12 (5&6): 661–671, Hemoglobin
   Google Scholar
• Petkov G. H., Efremov G. D., Efremov D. G., Dimovski A., Tchaicarova P., Tchaicarov R., Rogina B., Agarwal S., Kutlar A., Kutlar F., Reese A. L., Stoming T. A., Huisman T. H.J. β-Thalassemia in Bulgaria. Hemoglobin 1990; 14(1)25–33
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Jurici D., Petkov G. H., Huisman T. H.J. β-Thalassemia in Yugoslavia and Bulgariay. Hematol. Revs. 1992; 6: 83–95
   Google Scholar
• Dimovski A., Efremov D. G., Jankovic L., Juricic D., Zisovski N., Stojanovski N., Nikolov N., Petkov G. T., Reese A. L., Stoming T. A., Efremov G. D., Huisman T. H.J. β-Thalassemia in Yugoslavia. Hemoglobin 1990; 14(1)15–24
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Molecular pathology of the hemoglobinopathies including the thalassemias; some examples observed in the population of The Netherlands. De Wetenschappelijle Betekenis van Hematologisch Onderzoek, P. Sonneveld, J. Lindemans. UniversiteitsErasmus Drukkerij, RotterdamThe Netherlands 1990; 27–48
   Google Scholar
• Cürük M. A., Yüregir G. T., Asadov C. D., Dadasova T., Gu L-H., Baysal E., Gu Y-C., Ribeiro M. L.S., Huisman T. H.J. Molecular characterization of β-thalassemia in Azerbaijan. Hum. Genet. 1992; 90: 417–419
   PubMed Web of Science ®Google Scholar
• Schiliro G., Di Gregorio F., Samperi P., Mirabile E., Liang R., Ç ürük M. A., Ye Z., Huisman T. H.J. Genetic heterogeneity of β-thalassemia in Southeast Sicily. Am. J. Hematol 1995; 48: 5–11
   PubMed Web of Science ®Google Scholar
• George E., Li H-J., Fei Y-J., Reese A. L., Baysal E., Cepreganova B., Wilson J. B., Gu L-H., Nechtman J. F., Stoming T. A., Liu J-C., Codrington J. F., Huisman T. H.J. Types of thalassemia among patients attending a large universityclinic in Kuala Lumpur, Malaysia. Hemoglobin 1992; 16(1)51–66
   PubMed Web of Science ®Google Scholar
• Cürük M. A., Molchanova T. P., Postnikov Yu. V., Pobedimskaya D. D., Liang R., Baysal E., Kolodey S., Smetanina N. S., Tokarev Yu. N., Rumyantsev A. G., Huisman T. H.J. β-Thalassemia alleles and unstable hemoglobin types amongRussian pediatric patients. Am. J. Hematol 1994; 46: 329–332
   PubMed Web of Science ®Google Scholar
• Brittenham G., Lozoff B., Harris J. W., Bapat V., Gravely M., Huisman T. H.J. halassemia in Southern India–interaction of genes forβ+-, β0-, and δ;0β0- thalassemia. Acta Haematol 1980; 63: 44–48
   PubMedGoogle Scholar
• Baysal E., Sharma S., Wong S. C., Jogessar V. B., Huisman T. H.J. Distribution of β-thalassemia mutations in three AsianIndian populations with distant geographical locations. Hemoglobin 1994; 18(3)201–209
   PubMed Web of Science ®Google Scholar
• Gilman J. G., Huisman T. H.J., Abels J. Dutch β0-thalassaemia: A 10 kilo-base DNA deletion associatedwith significant γ-chain production. Br. J. Haematol. 1984; 56: 339–348
   PubMed Web of Science ®Google Scholar
• Padanilam B. J., Felice A. E., Huisman T. H.J. Partial deletion of the 5′ β-globin gene region causesβ0-thalassemia in members of an american black family. Blood 1984; 64: 941–944
   PubMed Web of Science ®Google Scholar
• Diaz-Chico J. C., Yang K. G., Kutlar A., Reese A. L., Aksoy M., Huisman T. H.J. An ∼300 bp deletion involving part of the 55′ β-globingene region is observed in members of a Turkish family with β-thalassemia. Blood 1987; 70: 583–586
   PubMed Web of Science ®Google Scholar
• Dimovski A. J., Divoky V., Adekile A. D., Baysal E., Wilson J. B., Prior J. F., Raven J. L., Huisman T. H.J. A novel deletion of ∼27 kb including the β-globin geneand the locus control region 3′HS-1 regulatory sequence: β0-thalassemiaor hereditary persistence of fetal hemoglobin. Blood 1994; 83(3)822–827
   PubMed Web of Science ®Google Scholar
• Beris Ph., Miescher P. A., Diaz-Chico J. C., Han I-S., Kutlar A., Hu H., Wilson J. B., Huisman T. H.J. Inclusion-body β-thalassemia trait in a Swiss family iscaused by an abnormal hemoglobin (Geneva) with an altered and extended βchain carboxy-terminus due to a modification in codon β114. Blood 1988; 72: 801–805
   PubMed Web of Science ®Google Scholar
• Negri Arjona S., Maldonado Eloy-Garcia J., Gu L-H., Smetanina N. S., Huisman T. H.J. The dominant β-thalassaemia in a Spanish family is dueto a frameshift that introduces an extra CGG codon (=Arginine) at the 55′end of the second exon. Br. J. Haematol. 1996; 93: 841–844
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Punt K., Schaad J. D.G. Thalassemia minor associated with hemoglobin-B2 heterozygosity. A Family Report. Blood 1961; 17: 747–757
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Haemoglobin A2′ and the linked occurrence of Hb-A2′ and thalassaemia in one family. Proceedings of the Haemoglobin-Colloquium, H. Lehmann, K. Betke, ViennaAustria 1961; 73
   Google Scholar
• Dimovski A. J., Efremov D. G., Gul L-H., Huisman T. H.J. The relative levels of βA and βS mRNAs in Hb S heterozygotesand in patients with Hb S-β+-thalassaemia or Hb S-β+-HPFH combinations. Br. J. Haematol. 1994; 87: 353–356
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Gu L-H., Leonova J. Ye., Huisman T. H.J. Sickle cell anemia identified in a multiple-transfused patientthrough analysis of mRNA with an RT-PCR-based technique. Acta Haematol. 1995; 93: 105–107
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Huisman T. H.J. mRNA Analysis in reticulocytes of subjects with Hb D, Hb PortoAlegre, Hb E, and different types of unstable hemoglobin variants. Am. J. Hematol. 1996; 52: 258–264
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Gu L-H., Schiliró G., Di Cataldo A., Testa R., Jakovlevska Z., Efremov G. D., Huisman T. H.J. The relative Llevels of α-, β-, and γ-mRNAfrom patients with severe and intermediate β-thalassemia major. Acta Haematol. 1997; 97: 205–210
   PubMed Web of Science ®Google Scholar
• Molchanova T. P., Smetanina N. S., Huisman T. H.J. The importance of the 3′ untranslated region for the expressionof the α-globin genes. Hemoglobin 1996; 20(1)41–54
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Leonova J. Ye., Levy N., Huisman T. H.J. Identification of several α-globin gene variations ina small laotian family. Acta Haematol. 1995; 94: 144–147
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Leonova J. Y., Levy N., Huisman T. H.J. The α/β- and α2/α1-globin mRNA ratiosin different forms of α-thalassemia. Biochim. Biophys. Acta 1996; 1315: 188–192
   PubMed Web of Science ®Google Scholar
• Molchanova T. P., Smetanina N. S., Huisman T. H.J. A second, elongated, α2-globin mRNA is present in reticulocytesfrom normal persons and subjects with terminating codon or poly A mutations. Biochem. Biophys. Res. Commun. 1995; 214: 1184–1190
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Öner C., Baysal E., Öner R., Bozkurt G., Altay Ç., Gürgey A., Adekile A. D., Gu L-H., Huisman T. H.J. The relative levels of α2-, α-, and ζ-mRNAin Hb H patients with different deletional and nondeletional α-thalassemiadeterminants. Biochim. Biophys. Acta 1996; 1316: 176–182
   PubMed Web of Science ®Google Scholar
• Efremov D. G., Dimovski A. J., Sukurova E., Schiliro G., Zisovski N., Efremov G. D., Burrone O. R., Huisman T. H.J. γ-mRNA and Hb F levels in β-thalassaemia. Br. J. Haematol. 1994; 88: 311–317
   PubMedGoogle Scholar
• Smetanina N. S., Adekile A. D., Huisman T. H.J. Globin mRNA in β-thalassaemia heterozygotes with differentβ-thalassaemia alleles in heterozygotes for hereditary persistence offoetal haemoglobin. Acta Haematol. 1996; 96: 162–169
   PubMed Web of Science ®Google Scholar
• Smetanina N. S., Gu L-H., Simjanovska L., Momirovska A., Petkov G. H., Adekile A. D., Efremov G. D., Huisman T. H.J. α-, β-, and γ-mRNA levels in β-thalassemia;transcriptional and translational differences in heterozygotes, homozygotes,and compound heterozygotes. Hemoglobin 1997; 21(1)27–39
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., van der Helm H. J., Visser H. K.A., van Vliet G. Investigations on different haemoglobin types in some species of animals. Proceedings of the CIOMS Conference on Abnormal Haemoglobins, Istanbul,Turkey, 1957. BlackwellScientific Publications, OxfordEngland 1959; 181–201
   Google Scholar
• van Vliet G., Huisman T. H.J. Changes in the haemoglobin types of sheep as a response to anaemia. Biochem. J. 1964; 93: 401–409
   PubMed Web of Science ®Google Scholar
• Moore S. L., Godley W. C., van Vliet G., Lewis J. P., Boyd E., Huisman T. H.J. The production of hemoglobin C in sheep carrying the gene forhemoglobin A: hematologic aspects. Blood 1966; 28: 314–329
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. The In vivo production of hemoglobin C in ruminants. Part XII.Biosynthetic Phenomena unique to nonhuman species: further models for dissectionand regulation. Ann. N.Y. Acad. Sci. 1974; 241: 549–555
   PubMedGoogle Scholar
• Blunt M. H., Huisman T. H.J., Lewis J. P. The production of hemoglobin C in adult sheep and goats. Austral. J. Exp. Biol. Med. Sci. 1969; 47: 601–611
   PubMedGoogle Scholar
• Lewis J. P., Miller A., Huisman T. H.J. The influence of antiserum to human erythropoietin on the productionof hemoglobin C in goats. Proc. Soc. Exp. Biol. Med. 1970; 134: 990–992
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Lewis J. P., Blunt M. H., Adams H. R., Miller A., Dozy A. M., Boyd E. M. Hemoglobin c in newborn sheep and goats: A possible explanationfor its function and biosynthesis. Pediatr. Res. 1969; 3: 189–198
   PubMed Web of Science ®Google Scholar
• Abraham E. C., Stallings M., Huisman T. H.J. Synthesis of hemoglobin chains in adult and newborn goats: apossible influence of the βC synthesis on the production of α chains. Hemoglobin 1982; 6(2)131–142
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Miller A., Huisman T. H.J. Production of hemoglobin C in the moufflon (Ovis Musimon Pallas,1811) and the Barbary Sheep (Ammotragus Lervia Pallas, 1777) during experimentalanemia; amino acid composition of tryptic peptides from the βB and βCchains. Biochem. Genet. 1970; 6: 677–688
   Google Scholar
• Huisman T. H.J., Miller A. Hemoglobin types in Barbary Sheep (Ammotragus Lervia Pallas,1977); absence of βC production in a homozygous βC (na) animal duringsevere anemia. Proc. Soc. Exp. Biol. Med. 1972; 140: 815–819
   PubMed Web of Science ®Google Scholar
• Bell J. T., Jr., Huisman T. H.J. Hemoglobin types in an anemic cow. Am. J. Vet. Res. 1968; 29: 479–482
   Web of Science ®Google Scholar
• Blunt M. H., Blalock E., Kitchens J., Huisman T. H.J. Effect of severe hemorrhage on the hemoglobins of a Virginiawhite-tailed deer (Odocoileus Virginianus). Proc. Soc. Exp. Biol. Med. 1968; 127: 38–41
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Reynolds C. A., Dozy A. M., Wilson J. B. The structure of sheep hemoglobins. The amino acid compositionof the α and β chains of the hemoglobins A, B, and C. J. Biol. Chem. 1965; 240: 2455–2460
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Edwards W. C., McDaniel M., Dobbs M. M., Huisman T. H.J. The structure of sheep hemoglobins. II. The amino acid compositionsof the tryptic peptides of the non-α chains of hemoglobins A, B, C,and F. Arch. Biochem. Biophys. 1966; 115: 385–400
   Web of Science ®Google Scholar
• Huisman T. H.J., Adams H. R., Dimmock M. O., Edwards W. C., Wilson J. B. Structure of goat hemoglobins. I. structural studies of βchains of the hemoglobins of normal and anemic goats. J. Biol. Chem. 1967; 242: 2534–2541
   PubMed Web of Science ®Google Scholar
• Adams H. R., Boyd E. M., Wilson J. B., Miller A., Huisman T. H.J. The structure of goat hemoglobins. III. hemoglobin D, a βchain variant with one apparent amino acid substitution (21 Asp→His). Arch. Biochem. Biophys. 1968; 127: 398–405
   PubMed Web of Science ®Google Scholar
• Wrightstone R. N., Wilson J. B., Miller A., Huisman T. H.J. The structure of goat hemoglobins. IV. A third β chainvariant (βE) with three apparent amino acid substitutions. Arch. Biochem. Biophys. 1970; 138: 451–456
   PubMed Web of Science ®Google Scholar
• Bannister J. V., Bannister W. H., Wilson J. B., Lam H., Miller A., Huisman T. H.J. The structure of goat hemoglobins. V. A fourth β chainvariant (β-D-Malta; 69 Asp→Gly) with decreased oxygen affinity andoccurring at a high frequency in Malta. Hemoglobin 1979; 3(1)57–75
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Brandt G., Huisman T. H.J. The structure of sheep hemoglobins. III. structural studiesof the α chain of hemoglobin. A. J. Biol. Chem. 1968; 243: 3687–3692
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M., Wilson J. B., Efremov G. D., Vaskov B. Sheep hemoglobin D, an α chain variant with one apparentamino acid substitution (α15 Gly→Asp). Biochim. Biophys. Acta 1968; 160: 467–469
   PubMedGoogle Scholar
• Huisman T. H.J., Wilson J. B., Adams H. R. The heterogeneity of goat hemoglobin: evidence for the existenceof two nonallelic and one allelic α-chain structural genes. Arch. Biochem. Biophys. 1967; 121: 528–530
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Brandt G., Wilson J. B. The structure of goat hemoglobins. II. structural studies ofthe α chains of hemoglobins A and B. J. Biol. Chem. 1968; 243: 3675–3686
   PubMed Web of Science ®Google Scholar
• Garrick M. D., Huisman T. H.J. Gene duplication of the α chain of goat hemoglobins: evidencefrom a homozygous mutant. Biochim. Biophys. Acta 1968; 168: 585–587
   PubMed Web of Science ®Google Scholar
• Adams H. R., Wrightstone R. N., Miller A., Huisman T. H.J. Quantitation of hemoglobin α chains in adult and fetalgoats; gene duplication and the production of polypeptide chains. arch. Biochem. Biophys. 1969; 132: 223–236
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Adams H. R., Huisman T. H.J. The heterogeneity of the fetal hemoglobin of the goat. Biochim. Biophys. Acta 1969; 181: 367–372
   PubMedGoogle Scholar
• Blunt M. H., Kitchens J. L., Mayson S. M., Huisman T. H.J. Red cell 2, 3– diphosphoglycerate and oxygen affinityin newborn goats and sheep (35992). Proc. Soc. Exp. Biol. Med. 1971; 138: 800–803a
   PubMedGoogle Scholar
• Huisman T. H.J., Dasher G. A., Moretz W. H., Dozy A. M., Wilson J. B., van Vliet G. Studies of haemoglobin types in Barbary Sheep (Ammotragus Lervia). Biochem. J. 1968; 107: 745–751
   PubMed Web of Science ®Google Scholar
• Wilson J. B., Wrightstone R. N., Huisman T. H.J. Haemoglobin a chain duplication in Barbary Sheep, AmmotragusLervia, Pallas, 1777. Nature 1970; 226: 354–355
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Hemoglobin types in some domestic animals. Proceedings of the Xe European Congress, Polymorphismes BiochimiquesAnimaux,. ParisFrance 1966; 61–75
   Google Scholar
• Huisman T. H.J. Multiple α and β chain structural genes as a basis for hemoglobin heterogeneity of the adult goat. Proceedings of the XVII Colloquium, Protides of the BiologicalFluids, Bruges, Belgium. Pergamon Press, New York, NY, USA 1969; 241–248
   Google Scholar
• Huisman T. H.J. Structural aspects of fetal and adult hemoglobin from nonanemicruminants. Ann. N.Y. Acad. Sci. 1974; 241: 392–411
   PubMed Web of Science ®Google Scholar
• Blunt M. H., Huisman T. H.J. The haemoglobins of sheep. Composition and Function. The Blood of Sheep, M. H. Blunt. Springer-Verlag: Berlin-Heidelberg, New York 1975; 155–183
   Google Scholar
• Schroeder W. A., Shelton J. R., Shelton J. B., Apell G., Huisman T. H.J., Smith L. L., Carr W. R. Amino acid sequences in the β-chains of adult bovine hemoglobinsC-Rhodesia and D-Zambia. Arch. Biochem. Biophys. 1972; 152: 222–232
   PubMed Web of Science ®Google Scholar
• Harris M. J., Wilson J. B., Huisman T. H.J. Two hemoglobin phenotypes in the American bison (Bison Bison):A possible genetic explanation based on structural studies. Biochem. Genet. 1973; 9: 1–11
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Dozy A. M., Blunt M. B., Hayes F. A. The hemoglobin heterogeneity of the Virginia white-tailed deer:A possible genetic explanation. Arch. Biochem. Biophys. 1968; 127: 711–717
   PubMed Web of Science ®Google Scholar
• Harris M. J., Huisman T. H.J., Hayes F. A. Geographic distribution of hemoglobin variants in the white-taileddeer. J. Mammal. 1973; 54: 270–274
   PubMed Web of Science ®Google Scholar
• Harris M. J., Wilson J. B., Huisman T. H.J. Structural studies of hemoglobin a chains from virginia white-taileddeer. Arch. Biochem. Biophys. 1972; 152: 540–548
   Google Scholar
• Wong S. C., Huisman T. H.J. Viscosity and gelation studies in deer hemoglobins. Proc. Soc. Exp. Biol. Med. 1975; 150: 581–584
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J., Schillhorn van Veen J. M., Dozy A. M., Nechtman C. M. Studies on animal hemoglobins. II. The influence of inorganicphosphate on the physicochemical and physiological properties of the hemoglobinof the adult chicken. Biochim. Biophys. Acta 1964; 88: 352–366
   PubMedGoogle Scholar
• Huisman T. H.J., Schillhorn van Veen J. M. Studies on animal hemoglobins. III. the possible role of intercellularinorganic phosphate on the oxygen equilibrium of the hemoglobin of the developingchicken. Biochim. Biophys. Acta 1964; 88: 367–374
   PubMedGoogle Scholar
• Huisman T. H.J. Hematologic features and types of hemoglobin in the domestic pig. The Pig Model for Biomedical Research, W. J. Dodds, 1982; 41: 249–250, Fed. Proc.
   Google Scholar
• Dozy A. M., Reynolds C. A., Still J. M., Huisman T. H.J. Studies on animal hemoglobins. I. hemoglobins in turtles. J. Exp. Zool. 1964; 155: 343–348
   PubMedGoogle Scholar
• Crepreganova B., Wilson J. B., Webber B. B., Kjovkareska B., Efremov G. D., Huisman T. H.J. Heterogeneity of the hemoglobin of the Ohrid trout (Salmo L.Typicus). Biochem. Genet. 1992; 30: 385–399
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. Normal and abnormal hemoglobins. Advances in Clinical Chemistry. Academic Press, Inc., NewYork, NY, USA 1963; 6: 231–361
   Google Scholar
• Huisman T. H.J. Normal and abnormal hemoglobins. Advances in Clinical Chemistry. Academic Press, Inc., NewYork, NY, USA 1972; 15: 149–253
   Google Scholar
• Huisman T. H.J. Normal and abnormal hemoglobins. Handbook of Clinical Laboratory Data. The Chemical Rubber Co., Cleveland, OH, USA 1968
   Google Scholar
• Huisman T. H.J. Human hemoglobins. Biochemical Methods in Red Cell Genetics, J. J. Yunis. AcademicPress, Inc., New York, NY, USA 1969; 391–504
   Google Scholar
• Huisman T. H.J., Schroeder W. A. Genetic aspects of gamma chain synthesis. Proceedings of the International Symposium “Synthese, Struktur,und Funktion des Hämoglobins”, H. Martin, A. L. Novicki. BadNauheim, Germany, J.F. Lehmanns Verlag, MünchenGermany 1972; 217–224
   Google Scholar
• Huisman T. H.J. Human hemoglobin abnormalities. Am. Assoc. Clin. Chem. 1984; 1(8)1–18
   Google Scholar
• Efremov G. D., Huisman T. H.J. The laboratory diagnosis of haemoglobinopathies. Clinics in Haematology 1974; 3: 527–570
   Google Scholar
• Kutlar A., Huisman T. H.J. Detection of hemoglobinopathies. Techniques in Diagnostic Human Biochemical Genetics: a LaboratoryManual, F. A. Hommes. J. Wiley & Sons, Inc., NewYork, NY, USA 1991; 519–560
   Google Scholar
• Huisman T. H.J. Human hemoglobin. Blood Disease of Infancy and Childhood, 7th Edition, D. R. Miller, R. L. Baehner. Mosby-Year Book, Inc, St. Louis, MO, USA 1995; 385–414
   Google Scholar
• Huisman T. H.J. The structure and function of normal and abnormal hemoglobins. The Haemoglobinopathies, D. J. Weatherall, D. R. Higgs. W.B.Saunders Company, LondonEngland 1993; 6: 1–30, Bailliére'sClinical Haematology
   Google Scholar
• Huisman T. H.J. Past, present, and future of research and diagnostics of structural hemoglobin variants. Hemoglobinopathies and Todays Genetics, G J.B. van Ommen, R. Fodde, P. C. Giordano, M. Losekoot. Proceedings of the Boerhaave Symposium, LeidenThe Netherlands 1994; 1–9
   Google Scholar
• Huisman T. H.J. New procedures for the diagnosis of the hemoglobinopathies. Proceedings of the 7th Asian-Pacific Congress on Clinical Chemistry. BangkokThailand 1995; 91–98
   Google Scholar
• Huisman T. H.J. Changes of hemoglobin in anemia. Proceedings of the XI Colloquium, Protides of the BiologicalFluids, Brugge, Brussels. H. Peeters. Elsevier PublishingCompany, AmsterdamThe Netherlands 1964; 396–399
   Google Scholar
• Niazi G. A., Huisman T. H.J. (1977) Erythrocytes and hemoglobinvariants. Parts I and II. Proceedingsof the Royal Dutch Academy of Science, AmsterdamThe Netherlands, 1976. 80: 13–34, Series C
   Google Scholar
• Huisman T. H.J. Globin gene regulation. Hereditary Disease and Blood Transfusion, C. Th. Smit Sibinga, P. C. Das, E. Briët. KluwerAcademic Publishers, DordrechtTheNetherlands 1995; 30: 53–61, Developments in Hematology and Immunology
   Google Scholar
• Huisman T. H.J. Chromatography of hemoglobin variants. The Detection of Hemoglobinopathies, R. M. Schmidt, T. H.J. Huisman, H. Lehmann. CRC Press Critical Review, Cleveland, OH, USA 1974; 43–48, Lab.Sci.
   Google Scholar
• Huisman T. H.J. Separation and characterization of hemoglobins. ACS Symposium Series, No. 36, Clinical Chemistry, D. T. Foreman, R. W. Mattoon, 1976; 1–48
   Google Scholar
• Huisman T. H.J. Separation of hemoglobins and hemoglobin chains by highperformance liquid chromatography. Separation of Biopolymers and Supramolecular Structures, Z. Deyl, M. T.W. Hearn, 1987; 418: 277–304, J. Chromatogr.
   Google Scholar
• Schroeder W. A., Huisman T. H.J. Nonallelic structural genes and hemoglobin synthesis. Proceedings of the XIII International Congress of Hematology. MunichGermany 1970; 26–33
   Google Scholar
• Schroeder W. A., Huisman T. H.J. Human gamma chains: structural features. Cellular and Molecular Regulation of Hemoglobin Switching, G. Stamatoyannopoulos, A. W. Nienhuis. Grune and Stratton, NewYork, NY, USA 1979; 29–45
   Google Scholar
• Huisman T. H.J. The human fetal hemoglobins. Human Hemoglobins and Hemoglobinopathies; a review to 1981, R. G. Schneider, C. Charache, W. A. Schroeder. The University of TexasMedical Branch, Galveston, TX, USA 1980–1981;; 40: 29–42, TexasReports on Biology and Medicine
   Google Scholar
• Huisman T. H.J. The occurrence of γ chain variants and related anomalies in various populations of the world. Distribution and Evolution of Hemoglobin and Globin Loci, J. E. Bowman. Elsevier Science Publishing Co. Inc., AmsterdamThe Netherlands 1983; 4: 119–142, The University of Chicago SickleCell Center Hemoglobin Symposia
   Google Scholar
• Huisman T. H.J. A short review of human γ gene anomalies. Acta Haematol. 1987; 78: 80–84
   PubMed Web of Science ®Google Scholar
• Efremov G. D., Huisman T. H.J. The occurrence of α and β chain abnormal hemoglobins and β-thalassemia in European countries. Distribution and Evolution of Hemoglobin and Globin Loci, J. E. Bowman. Elsevier Science Publishing Co. Inc., AmsterdamThe Netherlands 1983; 4: 315–344, The University of Chicago SickleCell Center Hemoglobin Symposia
   Google Scholar
• Huisman T. H.J. A short review of the different forms of α-, β-, δβ- and γ-thalassemia. Proceedings of the North Cyprus Symposium on Abnormal Hemoglobinsand Thalassemia, M. Aksoy, T. H.J. Huisman. Scientific and TechnicalResearch Council of Turkey, AnkaraTurkey 1984; 22–39
   Google Scholar
• Huisman T. H.J. Silent β-thalassemia and thalassemia intermedia. Haematologica 1990; 75: 1–8
   PubMed Web of Science ®Google Scholar
• Huisman T. H.J. (1996) Molecular genetics of α-thalassemia. Proceedings of the 26th Congress of the InternationalSociety of Haematology, Singapore, August, 1996, 233–236
   Google Scholar
• Jonxis J. H.P., Huisman T. H.J. A Laboratory Manual of Abnormal Haemoglobins.Revised Edition. BlackwellScientific Publications, OxfordEngland 1968
   Google Scholar
• Schroeder W. A., Huisman T. H.J. The Chromatography of Hemoglobin. Marcel Dekker,Inc., New York, NY, USA 1980; 9, Clinical and Biochemical Analysis
   Google Scholar
• Huisman T. H.J., Carver M. F.H., Efremov G. D. A Syllabusof Human Hemoglobin Variants (1996). The Sickle Cell Anemia Foundation, Augusta, GA, USA 1996, (http://globin.cse.psu.edu)
   Google Scholar
• Huisman T. H.J., Carver M. F.H., Baysal E. A Syllabus of Thalassemia Mutations(1997). TheSickle Cell Anemia Foundation, Augusta, GA,USA 1997, (http://globin.cse.psu.edu)
   Google Scholar
• Huisman T. H.J., Carver M. F.H., Efremov G. D. A Syllabusof Human Hemoglobin Variants. (Second Edition), The Sickle Cell Anemia Foundation, Augusta, GA, USA 1998, (http://globin.cse.psu.edu)
   Google Scholar
• Huisman T. H.J., Carver M. F.H., Efremov G. D. A Supplementto the Hemoglobin and Thalassemia Syllabi. The Sickle Cell Anemia Foundation, Augusta, GA, USA 1998, (http://globin.cse.psu.edu)
   Google Scholar