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. 1984 Feb 1;217(3):767–771. doi: 10.1042/bj2170767

Organic phosphates increase the solubility of avian haemoglobin D and embryonic chicken haemoglobin.

R Baumann, E Goldbach, E A Haller, P G Wright
PMCID: PMC1153280  PMID: 6424651

Abstract

The isolated minor haemoglobin fractions (haemoglobin D) of ostrich, chicken and duck haemoglobin, which constitute about 30% of total intracellular haemoglobin, form crystalline aggregates upon deoxygenation at physiological temperature, ionic strength and pH and at haemoglobin concentrations even well below those present in the red cell. The aggregation is reversed by oxygenation, and can be inhibited by addition of organic phosphates or the corresponding major haemoglobin fraction in a stoichiometric ratio of 1:1. Embryonic haemoglobin from chicken has similar characteristics with respect to its solubility. The results indicate close functional homology of alpha D and embryonic pi-chains as well as a novel role for organic phosphates in the regulation of haemoglobin function.

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Selected References

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

  1. Arnone A., Perutz M. F. Structure of inositol hexaphosphate--human deoxyhaemoglobin complex. Nature. 1974 May 3;249(452):34–36. doi: 10.1038/249034a0. [DOI] [PubMed] [Google Scholar]
  2. Aschauer H., Sanguansermsri T., Braunitzer G. Embryonale Hämoglobine des Menschen: Die Primärstruktur der zeta-Ketten. Hoppe Seylers Z Physiol Chem. 1981 Aug;362(8):1159–1162. [PubMed] [Google Scholar]
  3. Bartlett G. R., Borgese T. A. Phosphate compounds in red cells of the chicken and duck embryo and hatchling. Comp Biochem Physiol A Comp Physiol. 1976;55(3):207–210. doi: 10.1016/0300-9629(76)90132-8. [DOI] [PubMed] [Google Scholar]
  4. Benesch R. E., Edalji R., Benesch R., Kwong S. Solubilization of hemoglobin S by other hemoglobins. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5130–5134. doi: 10.1073/pnas.77.9.5130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Braunitzer G., Godovac J. Hemoglobins, XLV. The amino acid sequence of pheasant (Phasianus colchicus colchicus) hemoglobins. Hoppe Seylers Z Physiol Chem. 1982 Mar;363(3):229–238. doi: 10.1515/bchm2.1982.363.1.229. [DOI] [PubMed] [Google Scholar]
  6. Brown J. L., Ingram V. M. Structural studies on chick embryonic hemoglobins. J Biol Chem. 1974 Jun 25;249(12):3960–3972. [PubMed] [Google Scholar]
  7. Bruns G. A., Ingram V. M. The erythroid cells and haemoglobins of the chick embryo. Philos Trans R Soc Lond B Biol Sci. 1973 Oct 25;266(877):225–305. doi: 10.1098/rstb.1973.0050. [DOI] [PubMed] [Google Scholar]
  8. Brygier J., De Bruin S. H., Van Hoof M. K., Rollema H. S. The interaction of organic phosphates with human and chicken hemoglobin. Eur J Biochem. 1975 Dec 15;60(2):379–383. doi: 10.1111/j.1432-1033.1975.tb21013.x. [DOI] [PubMed] [Google Scholar]
  9. Chapman B. S., Tobin A. J., Hood L. E. Complete amino acid sequences of the major early embryonic alpha-like globins of the chicken. J Biol Chem. 1980 Oct 10;255(19):9051–9059. [PubMed] [Google Scholar]
  10. Czelusniak J., Goodman M., Hewett-Emmett D., Weiss M. L., Venta P. J., Tashian R. E. Phylogenetic origins and adaptive evolution of avian and mammalian haemoglobin genes. Nature. 1982 Jul 15;298(5871):297–300. doi: 10.1038/298297a0. [DOI] [PubMed] [Google Scholar]
  11. Drysdale J. W., Righetti P., Bunn H. F. The separation of human and animal hemoglobins by isoelectric focusing in polyacrylamide gel. Biochim Biophys Acta. 1971 Jan 19;229(1):42–50. doi: 10.1016/0005-2795(71)90315-1. [DOI] [PubMed] [Google Scholar]
  12. Fermi G. Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. J Mol Biol. 1975 Sep 15;97(2):237–256. doi: 10.1016/s0022-2836(75)80037-4. [DOI] [PubMed] [Google Scholar]
  13. Isaacks R. E., Harkness D. R., Froeman G. A., Goldman P. H., Adler J. L., Sussman S. A., Roth S. Studies on avian erythrocyte metabolism--II. Relationship between the major phosphorylated metabolic intermediates and oxygen affinity of whole blood in chick embryos and chicks. Comp Biochem Physiol A Comp Physiol. 1976;53(2):151–156. doi: 10.1016/s0300-9629(76)80046-1. [DOI] [PubMed] [Google Scholar]
  14. Jelkmann W., Bauer C. Regulation of red cell DPG metabolism in fetuses and adults. Acta Biol Med Ger. 1981;40(4-5):661–664. [PubMed] [Google Scholar]
  15. John M. E. Structural, functional and conformational properties of rat hemoglobins. Eur J Biochem. 1982 May 17;124(2):305–310. doi: 10.1111/j.1432-1033.1982.tb06592.x. [DOI] [PubMed] [Google Scholar]
  16. Morrow J. S., Wittebort R. J., Gurd F. R. Ligand-dependent aggregation of chicken hemoglobin AI. Biochem Biophys Res Commun. 1974 Oct 8;60(3):1058–1065. doi: 10.1016/0006-291x(74)90420-3. [DOI] [PubMed] [Google Scholar]
  17. Noguchi C. T., Schechter A. N. Inhibition of sickle hemoglobin gelation by amino acids and related compounds. Biochemistry. 1978 Dec 12;17(25):5455–5459. doi: 10.1021/bi00618a020. [DOI] [PubMed] [Google Scholar]
  18. Riggs A. Factors in the evolution of hemoglobin function. Fed Proc. 1976 Aug;35(10):2115–2118. [PubMed] [Google Scholar]
  19. Rossi-Bernardi L., Roughton F. J. The specific influence of carbon dioxide and carbamate compounds on the buffer power and Bohr effects in human haemoglobin solutions. J Physiol. 1967 Mar;189(1):1–29. doi: 10.1113/jphysiol.1967.sp008152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Saha A., Ghosh J. Comparative studies on avian hemoglobins. Comp Biochem Physiol. 1965 Jun;15(2):217–235. doi: 10.1016/0010-406x(65)90348-8. [DOI] [PubMed] [Google Scholar]
  21. Takei H., Ota Y., Wu K., Kiyohara T., Matsuda G. Amino acid sequence of the alpha chain of chicken AI hemoglobin. J Biochem. 1975 Jun;77(6):1345–1347. [PubMed] [Google Scholar]

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