The Role of Lectins in Blood Group Serology

References

• Boyd W. C., Shapleigh E. Specific precipitating activity of plant agglutinins (lectins). Science 1954; 119: 419
   PubMed Web of Science ®Google Scholar
• Prokop O., Uhlenbruck G., Kohler W. A new source of antibody-like substances having anti-blood group specificity. A discussion of the specificity of the Helix agglutinins. Vox Sang. 1968; 14: 321
   Google Scholar
• Gold E. R., Balding P. Receptor Specific Proteins—Plant and Animal Lectins. Excerpta Med., Amsterdam 1975
   Google Scholar
• Stillmark H. Über Rizin, ein giftiges Ferment aus Samen von Ricinus communi L., und einigen anderen Euphorbiaceen. Inaugaral Dissertation, Dorpat 1888
   Google Scholar
• Boyd W. C., Reguera R. M. Hemagglutinating substances for human cells in various plants. J. Immunol. 1949; 62: 333
   Google Scholar
• Renkonen K. O. Studies of hemagglutinins present in some representatives of the family of. Leg-uminosae, Ann. Med. Exp. Biol. Fenn. 1948; 26: 66
   Google Scholar
• Cazal P., Laularie M. Reserches sur quelques phyto-agglutinins specifiques des groupes sanguins ABO. Acta Haematol. 1952; 8: 73
   Google Scholar
• Ottensooser F., Silberschmidt K. Hemagglutinin anti-N in plant seeds. Nature (London) 1953; 172: 914
   Google Scholar
• Bird G. W. G. Specific agglutinating activity for human red blood corpuscles in extracts of. Dolichos biflorus, Curr. Sci. 1951; 20: 298
   Google Scholar
• Goldstein I. J., Hayes C. E. Advances in Carbohydrate Chemistry and Biochemistry, R. S. Tipton, D. Horton. Academic Press, New York 1978; 35, 127
   Google Scholar
• Wolpert J. S., Albersheim P. Host-symbiont interactions. 1. The lectins of legumes interact with the O-antigen-containing lipopolysaccharides of their symbiont Rhizobia. Biochem. Biophys. Res. Commun. 1976; 70: 729
   PubMedGoogle Scholar
• Fountain D. W., Foard D. E., Replogle W. D., Yang W. K. Lectin release by soybean seeds. Science 1977; 197: 1185
   Google Scholar
• Sharon N. Lectins. Sci. Am. 1977; 236: 108
   PubMed Web of Science ®Google Scholar
• Partridge J., Shannon L., Gumpf D. A barley lectin that binds free amino sugars. I. Purification and characterization. Biochim. Biophys. Acta 1976; 451: 470
   Web of Science ®Google Scholar
• Race R. R., Sanger R. Blood Croups in Man. Blackwell Scientific, Oxford 1975
   Google Scholar
• Murphy L. A. Ph.D. dissertation, University of Michigan. 1978
   Google Scholar
• Boyd W. C, Waszczenko-Zacharczenzko E., Goldwasser S. List of plants tested for hemagglutinaling activity. Transfusion (Philadelphia) 1961; 1: 374
   PubMedGoogle Scholar
• Judd W. J. The use of purified lectins in immunohematology. Transfusion (Philadelphia) 1979; 19: 768
   Google Scholar
• Prokop O., Schlessinger D., Rackwitz A. Über eine thermostabile “antibody-like substance” (anti-A) bei Helix pomatia und deren Herkunft. Z. Immunitaetsforsch. Allerg. Klin. Immunol. 1965; 129: 402
   Google Scholar
• Gold E. R., Thompson T. E. Serological differences between related species of snails. I. Revealed by passive agglutination tests. Vox Sang. 1969; 16: 63
   Google Scholar
• Tovey G. H., Lockyer W. J. Valuable new sources of anti-A and anti-B. J. Med. Lab. Technol. 1969; 26: 264
   Google Scholar
• Cann G. B. A laboratory evaluation of the hemagglutinating substance from the snail Helix aspersa. J. Med. Lab. Technol. 1974; 31: 11
   Google Scholar
• Voak D., Todd G. M., Pardoe G. I. A study of the serological behaviour and nature of the anti-B/P/P* activity of the Salmonidaeroe protectins. Vox Sang. 1974; 26: 176
   Google Scholar
• Rees P., Cotton R., Holt P. D. J., Anstee D. J. Trout ova, an alternative source of anti-B. Med. Lab. Sci. 1976; 33: 13
   Google Scholar
• Downie D. M., Madin D. F., Voak D. An evaluation of the salmon anti-B reagent in manual and automated blood grouping. Med., Lab. Sci. 1977; 34: 319
   Google Scholar
• Pardoe G. I., Uhlenbruck G., Anstee D. J., Reifenberg U. On the specificity of the broad spectrum agglutinins. III. Heterophile agglutinins associated with anti-B specificity. Z. Immunitaetsforsch. Allerg. Klin. Immunol. 1970; 117: 220
   Google Scholar
• Chattoraj A., Boyd W. C. A specific anti-B lectin for routine diagnostic purposes. J. Immunol. 1966; 96: 898
   Google Scholar
• Boyd W. C. Lectins. Ann. N. Y. Acad. Sci. 1970; 169: 168
   PubMedGoogle Scholar
• Rogers D. J., Blunden G., Evans P. R. Ptilota plumosa, a new source of an anti-B blood group specific lectin. Med. Lab. Sci. 1977; 34: 193
   PubMedGoogle Scholar
• Makelit O., Makela P. Some new blood group specific phytagglutinins. Ann. Med. Exp. Biol. Fenn. 1956; 34: 402
   Google Scholar
• Gold E. R., unpublished observations, cited in Reference 3
   Google Scholar
• Hayes C. E., Goldstein I. J. An α-D-galactosyl-binding lectin from Bandeiraea simplicifolia seeds. J. Biol. Chem. 1974; 249: 1904
   PubMedGoogle Scholar
• Judd W. J., Steiner E. A., Friedman B. A., Hayes C. E., Goldstein I. J. Serological studies on an α-D-galactosyl-binding lectin from Bandeiraea simplicifolia seeds. Vox Sang. 1976; 30: 261
   Google Scholar
• Murphy L. A., Goldstein I. J. Five α-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolis seeds. J. Biol. Chem. 1977; 252: 4739
   PubMed Web of Science ®Google Scholar
• Iyer P. N., Wilkinson K. D., Goldstein I. J. An N-Acetyl-D-glucosamine-binding lectin from. Bandeiraea simplicifolia seeds. Arch. Biochem. Biophys. 1976; 177: 330
   Google Scholar
• Judd W. J., Beck M. L., Hicklin B. L., Iyer P. N., Goldstein I. J. BS 11 Lectin: a second hemagglutinin isolated from Bandeiraea simplicifolia seeds with affinity for type III polyagglutinable red cells. Vox Sang. 1977; 33: 246
   Google Scholar
• Judd W. J., Murphy L. A., Goldstein I. J., Campbell L., Nichols M. E. An anti-B reagent prepared from the α-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds. Transfusion 1978; 18: 274
   Google Scholar
• Voak D., Lodge T. W., Reed J. V. The enhancement of Ulex europaeus anti-H activity by human sera. Vox Sang. 1969; 17: 134
   Google Scholar
• Mo Uison P. L. Blood Transfusion in Clinical Medicine. Blackwell Scientific, Oxford 1972
   Google Scholar
• Issitt P. D., Issitt C. H. Applied Blood Croup Serology. Spectra Biologicals, Oxnard 1975
   Google Scholar
• Beattie K. M. in. A Seminar on Problems Encountered in Pretransfusion Tests, R.H. Walker. American Association of Blood Banks, Washington, DC 1972; 129
   Google Scholar
• Voak D., Lodge T. W. The demonstration of anti-I/H1-H activity in seed anti-H reagunts. Vox Sang. 1971; 20: 36
   Google Scholar
• Bird G. W. G. Heterogeneity of anti-H lectin. Rev. Fr. Transfus. Immuno-hematol. 1976; 19: 175
   Google Scholar
• Morgan W. J., Watkins W. M. The inhibition of hemagglutinins in plant seeds by human blood group substances and simple sugars. Br. J. Exp. Pathol. 1953; 34: 94
   Google Scholar
• Watkins W. M. Blood group substances. Science 1955; 152: 172
   Google Scholar
• Matsumoto I., Osawa T. On the specificity of various heterologous anti-H hemagglutinins. Vox Sang. 1976; 21: 584
   Google Scholar
• Bird G. W. G., Wingham J. Anti-H from Cerastium tomentosum seeds. A comparison with other seed anti-H agglutinins. Vox Sang. 1970; 19: 132
   Google Scholar
• Rogers D. J., Topliss J. A., Blunden G. Reactions of anti-B lectins with erythrocytes sensitized with lipopolysaccharides from. Escherichia coli OM Med. Lab. Sci. 1979; 36: 79
   Google Scholar
• Gerbal A., Maslet C, Salmon C. Immunological aspects of the acquired-B antigen. Vox Sang. 1975; 28: 398
   Google Scholar
• Anderson J. Production of a B character on human red cells by hemosensitization with purifie Escherichia coli O86 substance. Nature (London) 1961; 190: 730
   Google Scholar
• Oguchi Y., Kawaguchi T., Suzata T., Osawa T. The nature of human blood group A, eryth rocytes. Vox Sang. 1978; 34: 32
   Google Scholar
• Bird G. W. G. Agar gel studies of blood group specific substances in precipitins of plant origin. 1. The precipitins of Dolichos biflorus. Vox Sang. 1959; 4: 307
   Google Scholar
• Gillespie E. M., Gold E. R. Weakening of the B antigen by the presence of A1 as shown by reactions with Fomes fomentarius (anti-B) extract. Vox Sang. 1960; 5: 497
   Google Scholar
• Reid M. E., Judd W. J. The effect of gene interaction on the A and B blood group antigens. J. Med. Lab. Technol. 1969; 26: 136
   Google Scholar
• Williams M. A., Voak D. Studies with ferritin labelled Dolichos biflorus lectin on the numbers and distribution of A sites on A1 and A2 erythrocytes, and on the nature of its specificity and enhance ment by enzymes. Vox Sang. 1972; 23: 427
   Google Scholar
• Boyd W. C, Bhatia H. M., Diamond M. A., Matsubara S. Quantitative study of the combination of Lima bean lectin with human erythrocytes. J. Immunol. 1962; 89: 463
   Google Scholar
• Economidou J., Hughes-Jones N. C, Gardner B. Quantitative measurements concerning A and B antigen sites. Vox Sang. 1967; 12: 321
   PubMedGoogle Scholar
• Voak K., Lodge T. W. The role of H in the development of A. Vox Sang. 1968; 15: 345
   Google Scholar
• Voak D., Stapleton R. R., Bowley C. C. A2AAl, a new variant of AA in two group A members of an English family. Vox Sang. 1968; 14: 18
   Google Scholar
• Voak D., Lodge T. W., Stapleton R. R., Fogg H., Roberts H. E. The incidence of H deficient A2 and A2B bloods and family studies on the AH/ABH status of an Aini and some new variant blood types (Ainil, AiniH. A2BMNWA and A2BNWA). VoxSang. 1970; 19: 73
   Google Scholar
• Gallasch E. Bombay phenotypes (Letter to the Editor). Vox Sang. 1978; 35: 436
   Google Scholar
• Weiner W., Lewis H. B. M., Moores P., Sanger R., Race R. R. A new geney, modifying the blood group antigen A. Vox Sang. 1957; 225
   Google Scholar
• Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc. Natl. Acad. Sci. 1975; 72: 2964
   PubMed Web of Science ®Google Scholar
• Furthmayr H. Structural comparisons of glycophorins and immunochemical analysis of genetical variants. Nature (London) 1978; 271: 519
   PubMed Web of Science ®Google Scholar
• Allen N. K., Brilliantine L. A survey of hemagglutinins in various seeds. J. Immunol. 1969; 102: 1295
   Google Scholar
• Nakajima H., Nakayama T. Anti-M lectin of Iberis amara L. Rep. Jpn. Natl. Res. Institute of Police Science 1968; 21: 111
   Google Scholar
• Okada T., Nakajima H. Anti-M lectin of Japanese radish. Rep. Jpn. Natl. Res. Institute of Police Science 1970; 23: 207
   Google Scholar
• Romanawska E. Reaction of M and N blood group substances natural and degraded with specific reagents of human and plant origin. Vox Sang. 1964; 9: 578
   Google Scholar
• Dahr W., Issitt P. D., Uhlenbruck G. New concepts of the MNSs blood group system. Human Blood Groups Mohn, F. J, R. W. Plunkett, R. K. Cunningham, R. M. Lambert. S. Karger, Basel 1977; 197
   Google Scholar
• Boyd W. C, Waszczenko-Zacharczenko E. Erythrocyte receptors for two “non-specific” lectins. Transfusion 1961; 1: 223
   Google Scholar
• Makela O. Studies on hemagglutinins in Leguminosae seeds. Ann. Med. Exp. Biol. Fenn. 1957; 35: 1, Suppl. 11
   PubMedGoogle Scholar
• Moon G. J., Wiener A. S. A new source of anti-N lectin: leaves of the Korean Vicia unijuga. VoxSang. 1974; 26: 167
   Google Scholar
• Bird G. W. G., Wingham J. Agglutinins for antigens of two different human blood group systems in the seeds of Moluccella laevis. Vox Sang. 1970; 18: 235
   Google Scholar
• Makela O., Cantell K. Destruction of M and N blood group receptors of human red cells by some influenza viruses. Ann. Med. Exp. Biol. Fenn. 1958; 36: 366
   Google Scholar
• Bird G. W. G., Wingham J. N-acetylneuraminic (sialic) acid and human group antigen structure. VoxSang. 1970; 18: 240
   Google Scholar
• Springer G. F., Ansell N. J. Inactivation of human erythrocyte agglutinogens M and N by influenza viruses and receptor destroying enzymes. Proc. Natl. Acad. Set. 1958; 44: 182
   PubMed Web of Science ®Google Scholar
• Uhlenbruck G. Possible genetical pathways in the MNSsUu system. Vox Sang. 1969; 16: 200
   Google Scholar
• Uhlenbruck G., Dahr W. Studies on lectins with a broad agglutination spectrum. XII. N-acetyl-D-galactosamine specific lectins from the seeds of Soja hispida, Bauhinia purpurea, Iberis amara, Moluccella laevis and Vicia graminea. Vox Sang. 1971; 21: 338
   Google Scholar
• Springer G. F., Huprikar S. V. On the biochemical and genetic basis of the blood group MN specificities. Haematologia 1972; 81(6)
   Google Scholar
• Springer G. F., Tegtmeyer H., Huprikar S. V. Anti-N reagents in the elucidation of the genetical basis of human blood group MN specificities. Vox Sang. 1972; 22: 325
   Google Scholar
• Lisowska E., Duk M. Effect of modification of amino groups of human erythrocytes M, N and Nvc blood group specificities. Vox Sang. 1975; 28: 392
   Google Scholar
• Walker M. E., Rubinstein P., Allen F. H., Jr. Biochemical genetics of MN. Vox Sang. 1977; 32: 111
   Google Scholar
• Lisowska E., Kordowicz M. Specific antibodies for desialyzed M and N blood group antigens. Vox Sang. 1977; 164
   Google Scholar
• Judd W. J., Issitt P. D., Pavone B. G., Anderson J., Aminoff D. Antibodies that define NANA-independent MN-system antigens. Transfusion 1979; 19: 12
   PubMed Web of Science ®Google Scholar
• Dahr W., Uhlenbruck G., Janssen E., Schmalisch R. Different N-terminal amino acids in the MN glycoprotein from MM and AWerythrocytes. Humangenetik 1977; 35: 335
   Google Scholar
• Wasniowska K., Drzeniek Z., Lisowska E. The amino acids of M and N blood group glyco-peptides are different. Biochem. Biophys. Res. Commun. 1977; 16: 385
   Google Scholar
• Thomas D. B., Winder R. J. Structural studies on human erythrocyte glycoproteins. Alkali-labile tetrasaccharides. J. Biol. Chem. 1969; 244: 5943
   PubMed Web of Science ®Google Scholar
• Steane E. A., Flanders J. Y., Steane S. M., Greenwalt T. J. The complexity of N specificity: a hypothesis correlating serology and biochemistry, preliminary data in support, and a proposal for nomenclature for the various M and N antigenic specificities. Transfusion 1978; 18: 645
   Google Scholar
• Anstee D. J. Blood group MNSs-active siaolglycoproteins of the human erythrocyte membrane. Immunobiology of the Red Cell Liss. in preparation, New York
   Google Scholar
• Gahmberg C. G., MyllyäK G., Leikola J., Pirkola A., Nordling S. Absence of the major sialoglycoprotein in the membrane of human En(a-) erythrocytes and increased glycosylation of band 3. J. Biol. Chem. 1976; 251: 6108
   PubMed Web of Science ®Google Scholar
• Kornfeld R., Kornfeld S. The structure of a phytohemaggultinin receptor site from human erythrocytes. J. Biol. Chem. 1970; 245: 2536
   PubMed Web of Science ®Google Scholar
• Dahr W., Issitt P. D., Moulds J., Pavone B. G. Further studies on the membrane glycoprotein defects of S-s-and En(a-) erythrocytes. Hoppe-Seyler's Z. Physiol. Chem. 1978; 359: 1217
   Google Scholar
• Tanner M. J. A., Anstee D. J., Judson P. A. A carbohydrate deficient membrane glycoprotein in human erythrocytes of phenotype S-s-. Biochem. J. 1977; 165: 157
   Google Scholar
• Fairbanks G., Steck T. L., Wallach D. F. H. Electrophoretic analysis of the major polypeptide of the human erythrocyte membrane. Biochemistry 1971; 10: 2606
   PubMed Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Narure (Xondon) 1970; 227: 680
   PubMed Web of Science ®Google Scholar
• Allen F. H., Jr., Corocan P. A., Ellis F. R. Some new observations on the MN system. Vox Sang. 1960; 5: 224
   Google Scholar
• Allen F. H., Jr., Madden H. J., King R. W. The M gene MU which produces M and U but no N, S or s. Vox Sang. 1963; 8: 549
   Google Scholar
• Dahr W., Uhlenbruck G., Knott H. Immunochemical aspects of the MNSs blood group system. J. Immunogenet. 1975; 2: 87
   Google Scholar
• Rolih S. D., Issitt P. D. Effects of trypsin on the Vicia graminea receptors of glycophorin A and B Transfusion. 1978; 18: 637
   Google Scholar
• Tokunaga E., Sasakawa S., Tamaka K., Kawamata H., Giles C. M., Ikin E. W., Poole J., Anstee D.J., Mawby W. J., Tanner M. J. A. Two apparently healthy Japanese individuals of type MM have erythrocytes which lack the MN and Ss-active sialoglycoproteins. J. Immunogener., in press
   Google Scholar
• Anstee D. J., Tanner M. J. A., Mawby W. J., Giles C. M. A new erythrocyte variant (Ph) containing an abnormal membrane sialoglycoprotein, in preparation
   Google Scholar
• Furuhjelm U., Myllyla G., Nevanlinna H. R., Nordling S., Pirkola A., Gavin J., Gooch A., Sanger R., Tippett P. The red cell phenotype En(a-) and anti-En: serological and physico-chemical aspects. Vox Sang. 1969; 17: 256
   PubMed Web of Science ®Google Scholar
• Damborough J., Dunsford I., Wallace J. A. The En° antigen and antibody. A genetical modification of human red cells affecting their blood group reactions. VoxSang. 1969; 17: 241
   Google Scholar
• Taliano V., Guevin R. M., Hebert D., Daniels G. L., Tippett P., Anstee D. J., Mawby W. J., Tanner M. J. A. The rare phenotype En(a-) in a French-Canadian family. Vox Sang, in press
   Google Scholar
• Anstee D. J., Barker D. M., Judson P. A., Tanner M. J. A. Inherited sialoglycoprotein deficiencies in erythrocytes of type En(a-). Br. J. Haematol. 1977; 35: 309
   Google Scholar
• Tanner M. J. A., Anstee D. J. The membrane changes in En(a-) erythrocytes. Biochem. J. 1976; 153: 271
   PubMed Web of Science ®Google Scholar
• Bird G. W. G., Wingham J. The action of seed and other reagents on En(a-) erythrocytes. Vox Sang. 1973; 24: 48
   Google Scholar
• Dahr W., Uhienbruck G., Leikola J., Wagstaff W. Studies on the membrane glycoprotein defect on En(a-) erythrocytes. III. N-terminal amino-acids of sialoglycoproteins from normal and En(a-) red cells. J. lmmunogenet. 1978; 5: 117
   Google Scholar
• Vengelen-Tyler V., Anstee D. J., Issitt P. D., Pavone B. G., Ferguson S. J., Mawby W. J., Tanner M. J. A., Blajchman M. A., Lorque P. Studies on the blood of an MivKhomozygote. Transfusion submitted 1979
   Google Scholar
• Langley J. W., Issitt P. D., Anstee D. J., McMahan M., Smith N., Pavone B. G., Tessel J. A., Carlin M. A. Another individual (J. R.) whose red cells appear to carry a hybrid sialoglycoprotein. Transfusion submitted 1979
   Google Scholar
• Dahr W., Uhienbruck G., Knott H. The defect of M° erythrocytes as revealed by sodium dodecysulphate-polyacrylamide gel electrophoresis. J. lmmunogenet. 1977; 4: 191
   Google Scholar
• Sturgeon P., Metaxas-Buhler M., Metaxas M. N., Tippett P., Ikin E. W. An erroneous exclusion of paternity in a Chinese family exhibiting the rare MNSs complexes Ma and Msmill. Vox Sang. 1970; 18: 395
   Google Scholar
• Nordling S., Sanger R., Gavin J., Furuhjelm U., Myllylä G., Metaxas M. N. Mk and M8: some serological and physicochemical observations. Vox Sang. 1969; 17: 300
   PubMed Web of Science ®Google Scholar
• Allen F. H., Jr., Corocan P. A., Kenton H. B., Breare N. M. a new blood group antigen in the MNS system. Vox Sang. 1958; 3: 81
   Google Scholar
• Anstee D. J., Tanner M. J. A. Genetic variants involving the major membrane sialoglycoproteins of human erythrocytes: studies on erythrocytes of type Mk, Miltenberger class V, and M8. Biochem. J. 1978; 175: 149
   Google Scholar
• Dahr W., Uhienbruck G. Structural properties of the human MN blood group antigen receptor sites. Hoppe-Seyler's Z. Physiol. Chem. 1978; 359: 835
   Google Scholar
• Dahr W., Longster G., Uhienbruck G., Schumacher K. Studies on Miltenberger class III, V, Ma and Mmill red cells.I. Sodium dodecylsulphate polyacrylamide gel electrophoresis investigations. Blur 1978; 37: 129
   Google Scholar
• Thomsen O. Ein vermehrungesfahiges Agens als Veranderer des isoagglutinatorischen Verhaitenes der roten Blutoperchen, eine bishe unbekannte Quelle der Fehlbestimmung. Z. Immunitaetsforsch Allerg. Klin. Immunol. 1927; 52: 85
   Google Scholar
• Hiibener G. Unterschunger Über Isoagglutination mit besonderer Berücksichtigung scheibarer Ab-weichungen vom Gruppenschema. Z. Immunitaetsforsch Allerg. Klin. Immunol. 1925; 45: 223
   Google Scholar
• Freidenreich V. The Thomsen Hemagglutinating Phenomenon. Levin and Munksgaard, Copenhagen 1930
   Google Scholar
• Levine P., Katzin E. M. Temporary agglutinability of red blood cells. Proc. Soc. Exp. Biol. N. Y. 1938; 39: 167
   Google Scholar
• Bangham A. D., Flemans R., Heard D. H., Seaman G. V. F. An apparatus for microelectrophoresis of small particles. Nature (London) 1958; 183: 642
   Google Scholar
• Steane E. A. Unpublished observations cited in Reference. 40: 262
   Google Scholar
• Aminoff D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem. J., SI 1961; 384
   Google Scholar
• Berman H. J., Smarto J., Issitt C. H., Issitt P. D., Marsh W. L., Jensen L. Tn-activation with acquired A-like antigen. Transfusion 1972; 12: 35
   PubMed Web of Science ®Google Scholar
• Bird G. W. G. Anti-T in peanuts. Vox Sang. 1964; 9: 748
   PubMed Web of Science ®Google Scholar
• Issitt P. D., Moulds J., Berman H. Some observations on the T, Tn and Sd' antigens and the antibodies that define them. Transfusion 1972; 12: 217
   Google Scholar
• Gunson H. H., Stratton F., Milliard G. W. An example of polyagglutinability due to the Tn antigen. Br. J. Haematol. 1970; 18: 309
   PubMed Web of Science ®Google Scholar
• Low B. A practical method using papain and incomplete Rh antibodies in routine Rh blood-grouping. Vox Sang. 1955; 5, O.S.
   Google Scholar
• Beck M. L., Marsh W. L. Red cell Sp, antigen change associated with in vivo polyagglutinability. Vox Sang. 1970; 19: 91
   Google Scholar
• Bird G. W. G., Wingham J., Beck M. L., Pierce S. R., Oates G. D., Pollack A. Th, a “new” form of erythrocyte polyagglutination. Lancet 1978; 1: 1215
   Google Scholar
• Bird G. W. G., Wingham J. Tk: a new form of red cell polyagglutination. Br. J. Haematol. 1972; 23: 759
   Google Scholar
• Inglis G., Bird G. W. G., Mitchell A. A. B., Milne G. R., Wingham J. Erythrocyte polyagglutination showing properties of both T and Tk, probably induced by Bacteroides fragilis infection. Vox Sang. 1975; 28: 314
   Google Scholar
• Inglis G., Bird G. W. G., Mitchel A. A. B., Milne G. R., Wingham J. Effect of Bacteroides fragilis on the human erythrocyte membrane; pathogenesis of Tk polyagglutination. J. Clin. Pathol. 1975; 28: 964
   Google Scholar
• Andreu G., Mativet S., Doinel C, Cartron J. P., Salmon C. In vitro Tk-polyagglutination—relations with acquired-B, 1 and i antigens Abstr. XV Congr. Int. Soc. Blood Transf. Librarie-Arnette, Paris 1978; 551
   Google Scholar
• Marsh W. L. The pseudo-B antigen, a study of its development. VoxSang. 1960; 5: 387
   Google Scholar
• Beck M. L., Walker R. H., Oberman H. A. Atypical polyagglutination associated with an acquired-B antigen. Transfusion 1971; 11: 296
   Google Scholar
• Judd W. J., McGuire-Mallory D., Anderson K., Heath E. J., Swanson J., Gray J. M., Oberman H. A. Concomitant T- and Tk-activation associated with acquired-B antigens. Transfusion 1979; 19: 293
   Google Scholar
• Moreau R., Dausset J., Bernard J., Moullec J. Anémie hémolytique acquise avec polyagglu-tinabilite des hemaites par un noveau facteur present dans le sérum humain normal (anti-Tn). Bull. Soc. Med. Hop. Paris Sceance May 17th, 1971
   Google Scholar
• Lalezari P., al-Mondhira H. Sialic acid deficiency of human red blood cells associated with persistent red cells, leukocyte and platelet polyagglutinability. Br. J. Haematol., 25: 399–408
   Google Scholar
• Cartron J. P., Andreu G., Cartron J., Bird G. W. G., Salmon C. Demonstration of T-transferase deficiency in Tn-polyagglutinable blood samples. Eur. J. Biochem. 1978; 92: HI
   Google Scholar
• Sturgeon P., McQuiston D. T., Taswell H. F., Allan C. J. Permanent mixed-field polyagglutinability (PMFP). I. Serological observations. Vox Sang. 1973; 25: 481
   Google Scholar
• Myllyla G., Furuhjelm U., Nordling S., Pirkola A., Tippett P., Gavin J., Sanger R. Per-sitent mixed field polyagglutinability. Electrokinetic and serological aspects. Vox Sang. 1971; 20: 7
   PubMed Web of Science ®Google Scholar
• Ness P. M., Garratty G., Morel P. A., Perkins H. A. Tn-polyagglutination preceding acute leukemia. Blood 1979; 54: 30
   PubMedGoogle Scholar
• Bird G. W. G., Wingham J. The M, N, and Nvc receptors of Tn erythrocytes. Vox Sang. 1974; 26: 171
   Google Scholar
• Bird G. W. G. Significant advances in lectins and polyagglutinable red cells. Plenary Sessions XV Congr. Int. Soc. Blood Transf. Librarie-Arnette, Paris, Paris 1978
   Google Scholar
• Bird G. W. G., Wingham J. Hemagglutinins from Salvia. VoxSang. 1974; 25: 163
   Google Scholar
• Bird G. W. G., Wingham J. More Saliva agglutinins. Vox Sang. 1976; 30: 217
   Google Scholar
• Bird G. W. G., Wingham J. Yet more Salvia agglutinins. Vox Sang. 1977; 32: 121
   Google Scholar
• Beck M. L., Hicklin B. L., Pierce S. R., Edwards R. L. Observations on leukocytes and platelets in six cases of Tn-polyagglutination. Med. Lab. Sci. 1977; 34: 325
   Google Scholar
• Cazal P., Monis M., Caubel J., Brives J. Polyagglutinabilitiéhéréditaire dominante: antigéne privé(Cad) correspondent à un anticorps public età une lectin Dolichos biflorus. Rev. Fr. Transf us. Immuno-hematol. 1968; 11: 209
   PubMedGoogle Scholar
• Sanger R., Gavin J., Tippett P., Teesdale P., Eldon K. Plant agglutinin for another blood group factor. Lancet 1970; 1: 1130
   Google Scholar
• Bird G. W. G., Wingham J. Some serological properties of the Cad receptor. Vox Sang. 1974; 20: 55
   Google Scholar
• Crookston J. H., Crookston M. C, Rosse W. Red cell abnormalities in HEMPAS (hereditary erythroblastic multinuclearity with a positive acidified serum test). Br. J. Haematol. 1972; 23: 81
   Google Scholar
• Gockennan J. P., Durocber J. R., Conrad M. E. The abnormal surface characteristics of the red cell membrane in congenital dyserythropoetic anemia type II (HEMPAS). Br. J. Haematol. 1975; 30: 383
   Google Scholar
• Bird G. W. G., Wingham J. The action of seed and other reagents on HEMPAS erythrocytes. Acta Haematol. 1976; 55: 174
   Google Scholar
• Graninger W., Rameis H., Fischer K., Poschmann A., Bird G. W. G., Wingham J., Neumann E. 'VA', a new type of polyagglutination characterized by depressed H receptors and associated with hemolytic anemia. I. Serological and hematological observations. Vox Sang. 1977; 32: 195
   Google Scholar
• Graninger W., Poschmann A., Fischer K., Schedl-Giovannoni I., Horander H., Klaushofer K. ‘VA’, a new type of polyagglutination characterized by depressed H receptors and associated with hemolytic anemia. II. Observations by immunofluorescence, electron microscope and biochemistry. VoxSang. 1977; 32: 201
   Google Scholar
• Beck M. L., Myers M. A., Moulds J., Pierce S. R., Hardman J., Wingham J., Bird G. W. G. Coexistent Tk and VA polyagglutinability. Transfusion 1978; 18: 680
   Google Scholar
• Naiki M., Marcus D. M. An immunochemical study of the human blood P1 P and P* glyco-sphingolipid antigens. Biochemistry 1975; 14: 4837
   Google Scholar
• Springer G. F., Desai P. R. Human blood group MN and precursor specificities: structural and biological aspects. Carbohydr. Res. 1975; 40: 183
   Google Scholar
• Uhlenbruck G., Pardoe G. I., Bird G. W. G. On the specificity of lectins with a broad hemagglutination spectrum. II. Studies on the nature of the T antigen and the specific receptors of Arachis hypogaea (ground nut). Z. Immunitaetsforsch. Allerg. Klin. Immunol. 1969; 138: 423
   Google Scholar
• Lotan R., Skutelsky E., Danon D., Sharon N. The purification, composition, and specificity of the anti-T lectin from the peanut (Arachis hypogaea). J. Biol. Chem. 1975; 250: 8518
   PubMed Web of Science ®Google Scholar
• Dahr W., Uhlenbruck G., Gunson H. H., van der Hart M. Molecular basis of Tn polyagglutinability. Vox Sang. 1975; 36
   Google Scholar
• Milliard G. W., Haworth C., Lee D. A case of atypical polyagglutinability due to Tk-transformation. Br. J. Haematol. 1978; 40: 571
   Google Scholar
• Zopf D. A., Tsai C. M., Ginsburg V. Studies on the carbohydrate receptors of cold agglutinins using synthetic antigens. Human Blood Groups Mohn, G. J, R. W. Plunkett, R. K. Cunningham, R. M. Lambert. S. Karger, Basel 1977; 172
   Google Scholar
• Mackvie S. E., Morton J., Pickles M. The reactions and inheritance of a new blood group antigen. Sd. VoxSang. 1967; 13: 485
   Google Scholar
• Morton J. A., Terry A. M. The Sd blood group antigen. Biochemical properties of urinary Sd. Vox Sang. 1970; 19: 151
   Google Scholar
• Boyd W. C, Green D. M., Fujinaga D. M., Drabik J. S., Waszczenko-Zacharczenko E. A blood factor, possibly new, detected by extracts of Arachis hypogaea. Vox Sang. 1959; 6: 456
   Google Scholar
• Schwarzfischer F., Liebrich K. Populationgenetische Unterschungen uber das Blutkorperchen-merkmal Gy. Blut 1962; 8: 161
   Google Scholar
• Prokop O., Uhlenbruck G. Human Blood and Serum Groups. McClaren and Sons, London 1969
   Google Scholar
• Jenkins G. C., Mollison P. L., Race R. R. Anti-D in Begonia punctata. Lancet 1961; 1: 1347
   Google Scholar
• Ikin E. W., Mourant A. E., Pugh V. W. An anti-Rh serum reacting differently with A and O red cells. Vox Sang. 1953; 3: 74, O.S.
   Google Scholar
• Issitt P. D. Serology and Genetics of Rh. Montgomery Scientific Publications, Cincinnati 1979
   Google Scholar
• Lockyer W. J., Gold E. R. ‘Natural’ anti-A and anti-B with small combining sites, together with anti-P, in the serum of the South African snake Python sebae. Med. Lab. Sci. 1977; 34: 303
   Google Scholar
• Plapp F. V., Kowalski M. A., Tilzer L., Brown P. J., Evans J., Cluger M. Partial purification of Rh. (D) antigen from Rh positive and negative erythrocytes. Proc. Natl. Acad. Sci. 1979; 76: 2964
   Google Scholar
• Schnitzler S., Muller G., Prokop O. Ein “neur” Antikorper: anti-Päfgefunden im Rogen von Rutilus rutilus. Z. Immun-Forsch. Allerg. Klin. Immunol. 1968; 134: 45
   Google Scholar
• Anstee D. J., Holt P. D. J., Pardoe G. I. Agglutinins from fish ova defining blood groups B and P. Vox Sang. 1973; 25: 347
   Google Scholar
• Voak D. J., Anstee D. J., Pardoe D. J. The α-galactose specificity of anti-P*. Vox Sang. 1975; 25: 253
   Google Scholar
• Schwarting G. A., Marcus D. M., Metaxas M. Identification of sialoparagloboside as the erythrocyte receptor for an ‘anti-p’ antibody. Vox Sang. 1977; 32: 257
   Google Scholar
• Chien S. M., Lemanski T., Poretz R. D. The anti-I activity of the Sophora japonica lectin. Immunochemistry 1974; 11: 501
   Google Scholar
• Rogers D. J. Lectin type agglutinins, with anti-BI and anti-H1 activity, from the ova of the black sea-bream Spondliosoma cantharus. Med. Lab. Sci. 1978; 35: 239
   Google Scholar
• Bird G. W. G., Wingham J. Anti-Cad lectin from the seeds of Leonurus cardiaca. Clin. Lab. Haematol. 1979; 1: 57
   Google Scholar
• Beck M. L. 1979, personal communication
   Google Scholar
• Murphy L. A. 1978, personal communication
   Google Scholar
• Moulds J. J., Judd W. J. 1977, unpublished observations
   Google Scholar
• Judd W. J. 1978, unpublished observations
   Google Scholar
• Beck M. L. 1976, personal communication
   Google Scholar
• Judd W. J. 1972, unpublished observations
   Google Scholar
• Beck M. L., Issitt P. D., Moulds J., Berman H. Transfusion 1972; 12: 217
   Google Scholar
• Ropars C. 1978, personal communication
   Google Scholar
• Harris P. 1979, personal communication
   Google Scholar
• Murphy L. A. 1977, personal communication
   Google Scholar
• Anstee D. J. 1977, personal communication
   Google Scholar
• Moulds J. J. 1979, personal communication
   Google Scholar
• Bird G. W. G. 1978, personal communication
   Google Scholar
• Judd W. J. 1979, unpublished observations
   Google Scholar