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. 1989 Jun 1;260(2):617–619. doi: 10.1042/bj2600617

Temperature- and pH-dependence of the oxygen-binding reaction of human fetal haemoglobin.

M L Doyle 1, S J Gill 1, R De Cristofaro 1, M Castagnola 1, E Di Cera 1
PMCID: PMC1138716  PMID: 2475101

Abstract

O2 binding to human haemoglobin F0 was studied at high haem concentrations (3 mM) in the temperature range 15-35 degrees C and in the pH range 6.8-8.7 at 25 degrees C. Comparison with O2 binding to human adult haemoglobin A0 under identical solution conditions reveals striking similarities in the Bohr effect and the enthalpy of oxygenation between the two haemoglobins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Castagnola M., Caradonna P., Cassiano L., Degen C., Lorenzin F., Rossetti D., Salvi M. L. Analysis of the globins from fast human haemoglobins by isoelectrofocusing on polyacrylamide gel rods. J Chromatogr. 1984 Apr 13;307(1):91–102. doi: 10.1016/s0378-4347(00)84075-x. [DOI] [PubMed] [Google Scholar]
  2. Castagnola M., Caradonna P., Salvi M. L., Rossetti D. Investigation of the heterogeneity of hemoglobin by cation-exchange chromatography on Bio-REX 70. J Chromatogr. 1983 Jan 14;272(1):51–65. doi: 10.1016/s0378-4347(00)86102-2. [DOI] [PubMed] [Google Scholar]
  3. Di Cera E., Doyle M. L., Connelly P. R., Gill S. J. Carbon monoxide binding to human hemoglobin A0. Biochemistry. 1987 Oct 6;26(20):6494–6502. doi: 10.1021/bi00394a031. [DOI] [PubMed] [Google Scholar]
  4. Di Cera E., Doyle M. L., Gill S. J. Alkaline Bohr effect of human hemoglobin Ao. J Mol Biol. 1988 Apr 5;200(3):593–599. doi: 10.1016/0022-2836(88)90545-1. [DOI] [PubMed] [Google Scholar]
  5. Di Cera E., Gill S. J. On the determination of species fractions from ligand-binding data. Application to human hemoglobin. Biophys Chem. 1988 Apr;29(3):351–356. doi: 10.1016/0301-4622(88)85057-9. [DOI] [PubMed] [Google Scholar]
  6. Dolman D., Gill S. J. Membrane-covered thin-layer optical cell for gas-reaction studies of hemoglobin. Anal Biochem. 1978 Jun 15;87(1):127–134. doi: 10.1016/0003-2697(78)90576-6. [DOI] [PubMed] [Google Scholar]
  7. Frier J. A., Perutz M. F. Structure of human foetal deoxyhaemoglobin. J Mol Biol. 1977 May 5;112(1):97–112. doi: 10.1016/s0022-2836(77)80158-7. [DOI] [PubMed] [Google Scholar]
  8. Gill S. J., Di Cera E., Doyle M. L., Bishop G. A., Robert C. H. Oxygen binding constants for human hemoglobin tetramers. Biochemistry. 1987 Jun 30;26(13):3995–4002. doi: 10.1021/bi00387a038. [DOI] [PubMed] [Google Scholar]
  9. Hayashi A., Suzuki T., Shin M. An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers. Biochim Biophys Acta. 1973 Jun 15;310(2):309–316. doi: 10.1016/0005-2795(73)90110-4. [DOI] [PubMed] [Google Scholar]
  10. Mann L. I., Romney S. L. The Bohr effect of fetal hemoglobin. Am J Obstet Gynecol. 1968 Jun 15;101(4):520–528. doi: 10.1016/0002-9378(68)90563-2. [DOI] [PubMed] [Google Scholar]
  11. SCHROEDER W. A., SHELTON J. R., SHELTON J. B., CORMICK J., JONES R. T. THE AMINO ACID SEQUENCE OF THE GAMMA CHAIN OF HUMAN FETAL HEMOGLOBIN. Biochemistry. 1963 Sep-Oct;2:992–1008. doi: 10.1021/bi00905a016. [DOI] [PubMed] [Google Scholar]
  12. Tyuma I., Imai K., Shimizu K. Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphates. Biochemistry. 1973 Apr 10;12(8):1491–1498. doi: 10.1021/bi00732a004. [DOI] [PubMed] [Google Scholar]
  13. WYMAN J., Jr LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. Adv Protein Chem. 1964;19:223–286. doi: 10.1016/s0065-3233(08)60190-4. [DOI] [PubMed] [Google Scholar]

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