Publication Cover
Hemoglobin
international journal for hemoglobin research
Volume 23, 1999 - Issue 4
23
Views
4
CrossRef citations to date
0
Altmetric
Original Article

Hb Bologna-St. Orsola [β146(HC3)His→Tyr]: a New High Oxygen Affinity Variant with Halved Bohr Effect and Highly Reduced Reactivity Towards 2,3-Diphosphoglycerate

, , , , , , , , & show all
Pages 353-359 | Received 13 Jan 1999, Accepted 25 Jun 1999, Published online: 07 Jul 2009

References

  • Beutler E. Red Cell Metabolism: A Manual of Biochemical Methods, 3rd edition. Grüne & Stratton Inc., New York, NYUSA 1984; 127–131
  • 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
  • Kynoch P. A.M., Lehmann H. Rapid estimation of glycosylate hemoglobin for routine purpose. The Lancet 1977; ii: 8027,16
  • Bohn B., Craescu G., Kister J., Bardakdjian J., Blouquit Y., Rosa J., Poyart C., Galacteros F. Structure-function of Hb Marseille-Long Island [α2β2 N-Methionyl-2(N A2) His←Pro]. Hemoglobin 1989; 13: 355–365
  • Kister J., Bardakdjian J., Blouquit Y., Bohn B., Galacteros F., Poyart C. Inhibition of oxygen-linked anion binding in Hb Camperdown [α2β2104(G6)Arg←Ser]. Hemoglobin 1989; 13: 567–578
  • Benesch R. E., Benesch R., Yung S. Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal. Biochem. 1973; 55: 245–248
  • Leone L., Monteleone M., Gabutti V., Amione C. Reversed-phase high-performance liquid chromatography of human Haemoglobin. J. Chromatogr. 1985; 321: 407–419
  • Clegg J. R., Naughton M. A., Weatherall D. J. Abnormal human hemoglobins. Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb Chesapeake and Hb J (Bangkok). J. Mol. Biol. 1966; 19: 91–108
  • Schroeder W. A. HPLC of globin chains and of peptides in the identification of hemoglobin variants. The Hemoglobinopathies, T. H.J. Huisman. Churchill-Livingstone, EdinburghScotland 1986; Vol. 15: 143–159, Methods in Hematology
  • Poncz M., Solowiejczyk D., Harpel B., Mory J., Schwartz E., Surrey S. Construction of human gene libraries from small amounts of peripheral blood: analyses of β-like globin genes. Hemoglobin 1982; 6: 27–36
  • Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn G. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 1988; 239: 487–491
  • Hultman T., Stahls S., Homes E., Uhlen M. Direct solid-phase sequencing of genomic and plasmid DNA, using magnetic beads as solid support. Nucleic Acids Res. 1989; 17: 4937–4946
  • Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. USA 1977; 74: 5463–5467
  • Imai K. Allosteric Effects in Haemoglobin. University Press, Cambridge, MAUSA 1982
  • Bunn H. F., Forget B. G. Hemoglobin: Molecular, Genetic and Clinical Aspects. W.B. Saunders Company, Philadelphia, PAUSA 1986
  • Ricco G., Roetto A., Sbaiz I., Girotti M., Rabino-Massa E. Preliminary reports on the oxymetry of dilute samples of human Hb A. J. Biol. Res. 1995; 71: 301–307
  • Ivaldi G., Scimè-Degani V., David O., Baffico M., Baldi M., Leone D., Mazzocco M., Leone L., Piga A., Furlan E., Ricco G. A new fast-moving variant causing erythrocytosisand mild hemolysis: Hb Gambara [P82(EF6)Lys←Glu]. Hemoglobin 1997; 21: 345–361
  • Imai K. Oxygen equilibrium characteristics of abnormal Hb Hiroshima (α2β2 143 Asp). Arch. Biochem. Biophys. 1968; 127: 543–547
  • Bare G. H., Bromberg P. A., Alben J. O., Brimhall B., Jones R. T., Mintz S., Rother I. Altered C-terminal salt bridges in Haemoglobin York causes high oxygen affinity. Nature 1976; 259: 155–156
  • Kosugi H., Weinstein A. S., Kikugawa K., Asakura T., Schroeder W. A. Characterization and properties of Hb York (β146 His←Pro). Hemoglobin 1983; 7: 205–226
  • Schneider R. G., Bremner J. E., Brimhall B., Jones R. T., Shih T-b. Hemoglobin Cowtown [β146(HC3) His←Leu]. A mutant with high oxygen affinity and erythrocytosis. Am. J. Clin. Pathol. 1979; 72: 1028–1032
  • Shih D. T-b., Jones R. T., Bonaventura J., Bonaventura C, Schneider R. G. Involvement of His HC3 (146) β in the Bohr effect of human hemoglobin. Studies of native N-Ethylmaleimide-treated Hemoglobin A and Hemoglobin Cowtown (β146 His←Leu). J. Biol. Chem. 1984; 259: 967–974
  • Wajcman H., Kilmartin J. V., Najman A., Labie D. Hemoglobin Cochin-Port Royal. Consequences of the replacement of the β chain C-terminal by an arginine. Biochim. Biophys. Acta 1975; 400: 354–364
  • Harano T., Harano K., Kushida Y., Imai K., Nishinakomura R., Matsunaga T. Hb Kodaira [β146(HC3)His←Glu], a new β chain variant with an amino acid substitution at the C-terminus. Hemoglobin 1992; 16: 85–91
  • Perutz M. F. Stereo-chemistry of cooperative effects in haemoglobin. Nature 1970; 228: 726–734
  • Perutz M. F., Muirhead H., Mazzarella F., Crowther R. A., Greer J., Kilmartin J. V. Identification of the residues responsible of the alkaline Bohr effect in haemoglobin. Nature 1969; 222: 1240–1243
  • Shih D. T-b, Perutz M. F. Influence of anions and protons on the Adair coefficients of Haemoglobins A and Cowtown His HC3(146) β-Leu. J. Mol. Biol. 1987; 195: 419–422
  • Shih D. T-b., Luisi Ben F., Miyazaki G., Perutz M. F., Nagal K. A mutagenic study of the allosteric linkage of His (HC3) 146β in haemoglobin. J. Mol. Biol. 1993; 230: 1291–1296
  • Perutz M. F., Shih D. T-b., Williamson D. The chloride effect in human haemoglobin. A new kind of allosteric mechanism. J. Mol. Biol. 1994; 239: 555–560
  • Nigen A. M., Manning J. M., Alben J. O. Oxygen-linked binding sites for inorganic ions. J. Biol. Chem. 1980; 255: 5525–5529
  • Perutz M. F., Kilmartin J. V., Nishikura K., Fogg J. H., Butler P. J., Rollema H. S. Identification of residues contributing to the Bohr effect in human haemoglobin. J. Mol. Biol. 1980; 138: 649–670
  • Kilmartin J. V., Wootton J. F. Inhibition of Bohr effect after removal of C-terminal histidines from haemoglobin beta-chains. Nature 1970; 228: 766–767
  • Winslow R. M., Swenberg M. L., Gross E., Chervenick P. A., Buchman R. R., Anderson W. F. Hemoglobin McKees Rocks (a2p2 145 Tyr←Term): a human “nonsense” mutation leading a shortened β-chain. J. Clin. Invest. 1976; 57: 772–781

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.