Recombinant Hemoglobin Variants

References

• Nagai K., Thergersen H. C. Nature 1984; 309: 810
   PubMed Web of Science ®Google Scholar
• Martin de Llano J. J., Schneewind O., Stetler G., Manning J. M. Proc. Natl. Acad. Sci. USA 1993; 90: 918
   PubMed Web of Science ®Google Scholar
• Shen T-J., Ho N. T., Simplaceanu V., Zou M., Green B. N., Tam M. F., Ho C. Proc. Natl. Acad. Sci. USA 1993; 90: 8108
   PubMed Web of Science ®Google Scholar
• Hernan R. A., Sligar S. G. J. Biol. Chem. 1995; 270: 26257
   PubMed Web of Science ®Google Scholar
• Adachi K., Konitzer P., Lai C. H., Surrey S. Protein Eng. 1992; 5: 807
   PubMedGoogle Scholar
• Adachi K., Rappaport E., Eck H. S., Konitzer P., Kim J., Surrey S. Polymerization and solubility of recombinant hemoglobins α2β26VAL (Hb S) and α2β26LEU (Hb LEU). Hemoglobin 1991; 15: 417
   PubMed Web of Science ®Google Scholar
• Adachi K., Konitzer P., Kim J., Welch N., Surrey S. Effects of β6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast. Biol. J. Chem. 1993; 268: 21650
   Web of Science ®Google Scholar
• Adachi K., Lai C. H., Konitzer P., Donahee M., Campbell A., Surrey S. Crystallization of recombinant hemoglobins with basic amino acid substitutions (Lys and Arg) at the p6 position. Blood 1994a; 84: 1309
   PubMed Web of Science ®Google Scholar
• Adachi K., Reddy L. R., Surrey S. Role of hydrophobicity of phenylalanine β85 and leucine β88 in the acceptor pocket for valine β6 during Hemoglobin S polymerization. J. Biol. Chem. 1994b; 269: 31563
   PubMed Web of Science ®Google Scholar
• Adachi K., Konitzer P., Surrey S. Role of y87 Gln in the inhibition of Hemoglobin S polymerization by Hemoglobin F. J. Biol. Chem. 1994c; 269: 9562
   PubMed Web of Science ®Google Scholar
• Adachi K., Konitzer P., Paulraj C. G., Surrey S. Role of Leu-β88 in the hydrophobic acceptor pocket for Val-β6 during Hemoglobin S polymerization. J. Biol. Chem. 1994d; 269: 17477
   PubMed Web of Science ®Google Scholar
• Adachi K., Reddy L. R., Reddy K. S., Surrey S. Mutational analysis of phenylalanine p85 in the valine β6 acceptor pocket during hemoglobin S polymerization. Protein Sci. 1995a; 4: 1272
   PubMed Web of Science ®Google Scholar
• Adachi K., Sabnekar P., Adachi M., Reddy L. R., Pang J., Reddy K. S., Surrey S. Polymerization of recombinant Hb S-Kempsey (deoxy-R state) and Hb S-Kansas (oxy-T state). J. Biol. Chem. 1995b; 270: 26857
   PubMed Web of Science ®Google Scholar
• Adachi K., Pang J., Konitzer P., Surrey S. Polymerization of recombinant Hemoglobin F yE6V and Hemoglobin F yE6V, yQ87T alone, and in mixtures with Hemoglobin S. Blood 1996a; 87: 1617
   PubMed Web of Science ®Google Scholar
• Adachi K., Pang J., Reddy L. R., Bradley L. E., Chen Q., Trifillis P., Schwartz E., Surrey S. Polymerization of three Hemoglobin A2 variants containing Val6 and inhibition of Hemoglobin S polymerization by Hemoglobin A2. J. Biol. Chem. 1996b; 271: 24557
   PubMed Web of Science ®Google Scholar
• Adachi K., Konitzer P., Pang J., Reddy K. S., Surrey S. Amino acids responsible for decreased 2, 3-biphosphosphoglycerate binding of fetal hemoglobin. Blood 1997; 90: 2916
   PubMed Web of Science ®Google Scholar
• Adachi K., Yamaguchi T., Pang J., Surrey S. Effects of increased anionic charge in the β-globin chain on assembly of hemoglobin in vitro. Blood 1998; 91: 1
   PubMed Web of Science ®Google Scholar
• Barrick D., Ho N. T., Simplaceanu V., Dahlquist F. W., Ho C. A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin. Nature Struct. Biol. 1997; 4: 78
   PubMedGoogle Scholar
• Baudin V., Pagnier J., Kiger L., Kister J., Schaad O., Bihoreau M. T., Lacaze N., Marden M. C., Edelstein S. J., Poyart C. Functional consequences of mutations at the allosteric interface in hetero-and homohemoglobin tetramers. Protein Sci. 1993; 2: 1320
   PubMed Web of Science ®Google Scholar
• Baudin V., Dumoulin A., Poyart C., Pagnier J. Hémoglobine humaine recombinante de faible affinitb pour l'oxygbne: effects additionnels de deux mutations. Trans. Clin. Biol. 1995; 2: 463
   PubMed Web of Science ®Google Scholar
• Baudin V., Kister J., Caron G., Jonval V., Poyart C., Pagnier J. The role of proline β5(A2) in the functional properties of human adult hemoglobin. Hemoglobin 1996; 20: 55
   PubMed Web of Science ®Google Scholar
• Bihoreau M. T., Baudin V., Marden M., Lacaze N., Bohn B., Kister J., Schaad O., Dumoulin A., Edelstein S. J., Poyart C., Pagnier J. Steric and hydrophobic determinants of the solubilities of recombinant sickle cell hemoglobins. Protein Sci. 1992; 1: 145
   PubMed Web of Science ®Google Scholar
• Cupane A., Leone M., Militello V., Friedman F. K., Koley A. P., Vasquez G. B., Brinigar W. S., Karavitis M., Fronticelli C. Modification of β-chain or β-chain heme pocket polarity by Val(E11) Thr substitution has different effects on the steric, dynamic, and functional properties of human recombinant hemoglobin. Biol J. Chem. 1997; 272: 26271
   Web of Science ®Google Scholar
• Doyle M. L., Lew G., De Young A., Kwiatkowski L., Wierzba A., Noble R. W., Ackers G. K. Functional properties of human hemoglobins synthesized from recombinant mutant P-globins. Biochemistry 1992; 31: 8629
   PubMed Web of Science ®Google Scholar
• Dumoulin A., Kiger L., Jiang R., Baudin V., Vasseur C., Sligar S. G., Marden M. C., Pagnier J., Poyart C. Loss of allosteric behavious in recombinant hemoglobin α2β292(F8)His αa: restoration upon addition of strong effectors. FEBS Lett. 1995; 374: 39
   PubMed Web of Science ®Google Scholar
• Fabry M. E., Sengupta A., Suzuka S. M., Costantini F., Rubin E. M., Hofrichter J., Christoph G., Manci E., Culberson D., Factor S. M., Nagel R. L. A second generation transgenic mouse model expressing both Hemoglobin S (HbS) and HbS-Antilles results in increased phenotypic severity. Blood 1995; 86: 2419
   PubMed Web of Science ®Google Scholar
• Fronticelli C., Brinigar W. S., Olson J. S., Bucci E., Gryczynski Z., O'Donnell J. K, Kowalczyk J. Recombinant human hemoglobin: modification of the polarity of the β-heme pocket by a valine67(E11) threonine mutation. Biochemistry 1993; 32: 1235
   PubMed Web of Science ®Google Scholar
• Fronticelli C., Sanna M. T., Perez-Alvarado G. C., Karavitis M., Lu A-L., Brinigar W. S. Allosteric modulation by tertiary structure in mammalian hemoglobins. Introduction of the functional characteristics of bovine hemoglobin into human hemoglobin by five amino acid substitutions. Biol J. Chem. 1995; 270: 30588
   Web of Science ®Google Scholar
• Himanen J-P., Schneider K., Chait B., Manning J. M. Participation and strength of interaction of lysine 95(β) in the polymerization of Hemoglobin S as determined by its sitedirected substitution by isoleucine. Mol. J. Biol. 1995; 270: 13885
   Google Scholar
• Himanen J-P., Mirra U. A., Chait B. T., Bookchin R. M., Manning J. M. A recombinant sickle hemoglobin triple mutant with independent inhibitory effects on polymerization. Biol. J. Chem. 1996; 271: 25152
   Web of Science ®Google Scholar
• Himanen J-P., Popowicz A. M., Manning J. M. Recombinant sickle hernoglobin containing a lysine substitution at Asp85(α): expression in yeast, functional properties, and participation in gel formation. Blood 1997; 89: 4196
   PubMed Web of Science ®Google Scholar
• Ho C., Willis B. F., Shen T-J., Ho N. T., Sun D. P., Tam M. F., Suzuka S. M., Fabry M. E., Nagel R. L. Roles of α114 and β87 amino acid residues in the polymerization of Hemoglobin S: implications for gene therapy. Mol. J. Biol. 1996; 263: 475
   PubMed Web of Science ®Google Scholar
• Ho C., Sun D. P., Shen T-J., Ho N. T., Zou M., Hu C-K, Sun Z-Y., Lukin J. A. Hemoglobins with low oxygen affinity and high cooperativity. Present and Future Perspective of Blood Substitutes, E. Tsuchida. Elsevier Science SA, LausanneSwitzerland 1998, in press
   Google Scholar
• Imai K., Fushitani K., Miyazaki G., Ishimori K., Kitagawa T., Wada Y., Morimoto H., Morishima I., Shih D. T-b., Tame J. Site-directed mutagenesis in haemoglobin functional role of tyrosine-42(C7)a at the α1-β2 interface. J. Mol. Biol. 1991; 218: 769
   PubMed Web of Science ®Google Scholar
• Ishimori K., Morishima I., Imai K., Fushitani K., Miyataki G., Shih D., Tame J., Pegnier J., Nigai K. NMR study of human mutant hemoglobins synthesized in Escherichai coli. J. Biol. Chem. 1989; 264: 14624
   PubMed Web of Science ®Google Scholar
• Kiger L., Baudin V., Desbois A., Pagnier J., Kister J., Griffon N., Henry Y., Poyart C., Marden M. C. Recombinant [Pheβ63]hemoglobin shows rapid oxidation of the β chains and low-affinity, non-cooperative oxygen binding to the a subunits. Eur. Biochem. J. 1997; 243: 365
   PubMedGoogle Scholar
• Kim H-W., Shen T-J., Sun D. P., Ho N. T., Madrid M., Tam M. F., Zou M., Cottam P. F., Ho C. Restoring allosterism with compensatory mutations in hemoglobin. Proc. Natl. Acad. Sci. USA 1994; 91: 11547
   PubMed Web of Science ®Google Scholar
• Kim H-W., Shen T-J., Sun D. P., Ho N. T., Madrid M., Ho C. A novel low oxygen affinity recombinant hemoglobin (a96VabTrp): switching quarternary structure without changting the ligation state. Mol. J. Biol. 1995; 246: 867
   Google Scholar
• Kim H-W., Shen T-J., HoMing N., Zou T., Tam M. F., Ho C. Contributions of asparagine at a97 to the cooperative oxygenation process of hemoglobin. Biochemistry 1996; 35: 6620
   PubMed Web of Science ®Google Scholar
• Lesecq S., Baudin V., Kister J., Marden M. C., Poyart C., Pagnier J. Functional studies and polymerization of recombinant hemoglobin Glu-α2β26(A3) Val/Glu-7(A4) Ala. J. Biol Chem. 1996; 271: 17211
   PubMed Web of Science ®Google Scholar
• Li X., Mirza U. A., Chait B. T., Manning J. M. Systematic enhancement of polymerization of recombinant sickle hemoglobin mutants: implications for transgenic mouse model for sickle cell anemia. Blood 1997; 90: 462
   Web of Science ®Google Scholar
• Luisi B. F., Nagai K. Crystallographic analysis of mutant human haemoglobins made in Escherichia coli. Nature 1986; 320: 555
   PubMed Web of Science ®Google Scholar
• Manning L. R., Jenkins W. T., Hess J. R., Vandegriff K., Winslow R. M., Manning J. M. Subunit dissociations in natural and recombinant hemoglobins. Protein Sci 1996; 5: 775
   PubMed Web of Science ®Google Scholar
• Martin de Llano J. J., Schneewind O., Stetler G., Manning J. M. Recombinant human sickle hemoglobin expressed in yeast. Proc. Natl. Acad. Sci. USA 1993a; 90: 918
   PubMed Web of Science ®Google Scholar
• Martin de Llano J. J., Jones W., Schneider K., Chait B. T., Manning J. M. Biochemical and funtional properties of recombinant human sickle hemoglobin expressed in yeast. Biol. J. Chem. 1993b; 268: 27004
   Web of Science ®Google Scholar
• Martin de Llano J. J., Manning J. M. Properties of a recombinant human hemoglobin double mutant: sickle hemoglobin with Leu-88(β) at the primary aggregation site substituted by Ala. Protein Sci 1994; 3: 1206
   PubMed Web of Science ®Google Scholar
• McCune S. L., Reilly M. P., Chomo M. J., Asakura T., Townes T. M. Recombinant human hemoglobins designed for gene therapy of sickle cell disease. Proc. Natl. Acad. Sci. USA 1994; 91: 9852
   PubMed Web of Science ®Google Scholar
• Militello V., Cupane A., Leone M., Brinigar W. S., Lu A-L., Fronticelli C. Dynamic properties of some P-chain mutant hemoglobins. Proteins. Struct., Funct., Genet. 1995; 22: 12
   PubMed Web of Science ®Google Scholar
• Mohvani N., Talarico T., Jain S., Bajwa W., Blackburn R., Nwosu V., Holland M., DeAngelo J., Privalle C., Keng T. Production, purification, and characterization of recombinant human Hemoglobin Rainier expressed in Saccharomyces cervisiae. Protein Expr. Purificat. 1996; 8: 447
   Google Scholar
• Nagai K., Perutz M. F., Poyart C. Oxygen binding properties of human mutant hemoglobins synthesized in Escherichai coli. Proc. Natl. Acad. Sci. USA 1985; 82: 7252
   PubMed Web of Science ®Google Scholar
• Nagai K., Luisi B., Shih D., Miyazaki G., Imai K., Poyart C., De Young A., Kwiatkowsky L., Noble R. W., Lin S-H., Yu N-T. Distal residues in the oxygen binding site of haemoglobin studied by protein engineering. Nature 1987; 329: 858
   PubMed Web of Science ®Google Scholar
• Pagnier J., Bihoreau M-T., Baudin V., Edelstein S. J., Poyart C. Polymerisation et solubilité des hémoglobines recombinantes α2β2 6 Gluαa (Hb Makassar) et α2β2 6 Glu αa, 23 Val lle. Comp. Rend. Acad. Sci. Paris 1993; 316: 431
   Google Scholar
• Reddy L. R., Reddy K. S., Surrey S., Adachi K. Role of hydrophobic amino acids at β85 and β88 in stabilizing F helix conformation in Hemoglobin S. J. Biol. Chem. 1996; 271: 24564
   PubMed Web of Science ®Google Scholar
• Reddy L. R., Reddy K. S., Surrey S., Adachi K. Role of β87 Thr in the β6 Val accepter site during deoxy Hb S polymerization. Biochemistry 1998, in press
   Web of Science ®Google Scholar
• Scheepens A., Mould R., Hofmann O., Brittain T. Some effects of post-translational N-terminal acetylation of the human embryonic globin protein. Biochem. J. 1995; 310: 597
   PubMed Web of Science ®Google Scholar
• Shih D. T.B., Luisi B. F., Miyazaki G., Perutz M. F., Nagai K. A mutagenic study of the allosteric linkage of His(HC3)143β in haemoglobin. Mol. J. Biol. 1993; 230: 1291
   PubMed Web of Science ®Google Scholar
• Sun D. P., Zou M., Ho N. T., Ho C. Contribution of surface histidyl residues in the a-chain to the Bohr effect on human normal adult hemoglobin: roles of global electrostatic effects. Biochemistry 1997; 36: 6663
   PubMed Web of Science ®Google Scholar
• Trifillis P., Adachi K., Yamaguchi T., Schwartz E., Surrey S. Expression studies of & globin gene alleles associated with reduced Hemoglobin A2 levels in Greek Cypriots. J. Biol. Chem. 1996; 271: 26931
   PubMed Web of Science ®Google Scholar
• Wagenbach M., O'Rourke K., Vitez L., Wieczorek A., Hoffman S., Durfee S., Tedesco J., Stetler G. Synthesis of wild type and mutant human hemoglobins in Saccharomyces cerevisiae. Biotechnology 1991; 9: 57
   PubMed Web of Science ®Google Scholar
• Weber R. E., Jessen T-H., Malte H., Tame J. Mutant hemoglobins (α119-Ala and β55-Ser): functions related to high-altitude respiration in geese. Appl. J. Physiol. 1993; 75: 2646
   PubMed Web of Science ®Google Scholar
• Yamashiro D. J., Adachi M., Konitzer P., Surrey S., Adachi K. Polymerization and instability of a recombinant hemoglobin containing valine β7. J. Biol. Chem. 1994; 269: 23996
   PubMed Web of Science ®Google Scholar
• Yanase H., Cahill S., Martin de Llano J. J., Manning L. R., Schneider K., Chait B. T., Vandegriff K. D., Winslow R. M., Manning J. M. Properties of a recombinant human hemoglobin with aspartic acid 99(β), an important intersubunit contact site, substituted by lysine. Protein Sci. 1994; 3: 1213
   PubMed Web of Science ®Google Scholar
• Yanase H., Manning L. R., Vandengriff K., Winslow R. M., Manning J. M. A recombinant human hemoglobin with asparagine-102(β) substituted by alanine has a limiting low oxygen affinity, reduced marginally by chloride. Protein Sci 1995; 4: 21
   PubMed Web of Science ®Google Scholar