Amino acids responsible for decreased 2, 3-biphosphosphoglycerate binding to fetal hemoglobin

Blood

Volumn 90, Issue 8, 1997, Pages 2916-2920

  Adachi, Kazuhiko ^a   Konitzer, Patrick ^b   Pang, Jian ^b   Reddy, Konda S ^b   Surrey, Saul ^b  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; AMINO ACID; GAMMA GLOBIN; HEMOGLOBIN F; HEMOGLOBIN S; HEMOGLOBIN VARIANT;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; ELECTROPHORESIS; GENE THERAPY; HUMAN; HUMAN CELL; OXYGEN AFFINITY; OXYGENATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; SICKLE CELL ANEMIA;

EID: 0030824944     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.8.2916     Document Type: Article

References (28)

1. Bunn HF, Forget BG: Hemoglobin: Molecular, Genetic and Clinical Aspects, Philadelphia, PA, Saunders, 1986, p 37
2. Allen DW, Wyman J, Smith CA: The oxygen equilibrium of foetal and adult human hemoglobin. J Biol Chem 203:81, 1953
3. Bauer C, Ludwig I, Ludwig M: Different effects of 2, 3 diphosphoglycerate and adenosine triphosphate on the oxygen affinity of adult and foetal human haemoglobin. Life Sci 7:1336, 1968
4. Bunn HF, Briel R: The interaction of 2, 3-diphosphoglycerate with various human hemoglobins. J Clin Invest 49:1088, 1970
5. Tomita SJ: Modulation of the oxygen equilibria of human fetal and adult hemoglobins by 2, 3-diphosphoglycerate acid. J Biol Chem 256:9495, 1981
6. Arnone A: X-ray diffraction study of binding of 2, 3-diphosphoglycerate to human deoxyhaemoglobin. Nature 237:146, 1972
7. Frier JA, Perutz MFJ: Structure of human foetal deoxyhemoglobin. J Mol Biol 112:97, 1977
8. Adachi K, Pang J, Konitzer P, Surrey S: Polymerization of recombinant Hb F γE6V and Hb F γE6V, γQ87T alone, and in mixtures with Hb S. Blood 87:1617, 1996
9. Adachi K, Konitzer P, Surrey S: Role of γ87 Gln in the inhibition of Hb S polymerization by Hb F. J Biol Chem 269:9562, 1993
10. Shackleton CH, Witkowska HE: Mass spectrometry in the characterization of variant hemoglobins, in Desiderio DM (ed): Mass Spectrometry: Clinical and Biomedical Applications. New York, NY, Plenum, 1994, p 135
11. Adachi K, Asakura T: Nucleation-controlled aggregation of deoxyhemoglobin S: Possible difference in the size of nuclei in different phosphate concentrations. J Biol Chem 254:7765, 1979
12. Festa RS, Asakura T: The use of oxygen dissociation curve analyzer in transfusion therapy. Crit Care Med 7:391, 1979
13. Adachi K, Konitzer P, Lai CH, Kim J, Surrey S: Oxygen-binding properties and mechanical stability of human hemoglobin made in yeast. Protein Eng 5:807, 1992
14. Hofmann OM, Mould RM, Brittain T: The incorporation of sulphaem into recombinant adult human haemoglobin produced in a yeast expression system. Protein Eng 7:281, 1994
15. Rossi-Fanelli A, Antonini E, Caputo A: Studies on the relations between molecular and functional properties of hemoglobin. I. The effect of salts on the molecular weight of human hemoglobin. J Biol Chem 236:391, 1961
16. Rossi-Fanelli A, Antonini E, Caputo A: Studies on the relations between molecular and functional properties of hemoglobin. II. The effect of salts on the oxygen equilibrium of human hemoglobin. J Biol Chem 236:397, 1961
17. O'Donnell S, Mandaro R, Shuster TM, Arnone A: X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. J Biol Chem 254:12204, 1979
18. II solutions. Pflugers Arch 376:169, 1978
19. Bonaventura J, Bonaventura C, Sullivan B, Ferruzzi G, McCurdy R, Fox J, Moo-Penn WF: Hemoglobin Providence: Functional consequences of two alterations of the 2, 3-diphosphoglycerate binding site at position beta 82. J Biol Chem 251:7563, 1976
20. International Hemoglobin Center: IHIC Variants list. Hemoglobin 19:39, 1995
21. Morimoto H, Lehman H, Perutz MF: Molecular pathology of human haemoglobin: Stereochemical interpretation of abnormal oxygen affinities. Nature 232:408, 1971
22. Brennan SO, Shaw JG, George PM, Huisman THJ: Posttranslational modification of β141 Leu associated with the β75(E19) Leu → Pro mutation in Hb Atlanta. Hemoglobin 17:1, 1993
23. Wilson CID, Cave RJ, Lehmann H, Close M, Imai K: Hemoglobin Warwickshire [β5(A2) Pro → Arg)], a possible fine tuning of 2, 3-BPG affinity by β5 Pro. FEBS Lett 176:331, 1984
24. 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 20:55, 1996
25. Giardina B, Brix O, Clementi ME, Scatena R, Nicoletti B, Ciccehtti R, Argentin G, Condo G: Differences between horse and human haemoglobins in effects of organic and inorganic anions on oxygen binding. Biochem J 266:897, 1990
26. Embury SH, Hebbel PR, Mohandas N, Steinberg MH: The Sickle Hemoglobins: Science and Medicine. New York, NY, Raven, 1994
27. 2 on the polymerization of hemoglobin S. Proc Natl Acad Sci USA 76:670, 1979
28. 2. J Biol Chem 271:24557, 1996