Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Oct;78(10):6076–6080. doi: 10.1073/pnas.78.10.6076

Structure of the zeta chain of human embryonic hemoglobin.

J B Clegg, J Gagnon
PMCID: PMC348980  PMID: 6171809

Abstract

The complete amino acid sequence of the zeta chain of human embryonic hemoglobin has been determined. It differs from human alpha globin at 57 of the 141 residues and several of the replacements are at positions of structural or functional importance, particularly in relationship to the Bohr effect and high intrinsic oxygen affinity which are characteristic of embryonic hemoglobins. The zeta-globin sequence is more closely related to other mammalian embryonic alpha-like globins than to human alpha, suggesting that there have been strong selective pressures to maintain these embryo-specific globins since their emergence several hundred million years ago.

Full text

PDF
6078

Selected References

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

  1. Abraham E. C., Reese A., Stallings M., Huisman T. H. Separation of human hemoglobins by DEAE-cellulose chromatography using glycine-KCN-NaC1 developers. Hemoglobin. 1976;1(1):27–44. doi: 10.3109/03630267609031020. [DOI] [PubMed] [Google Scholar]
  2. Baralle F. E., Shoulders C. C., Proudfoot N. J. The primary structure of the human epsilon-globin gene. Cell. 1980 Oct;21(3):621–626. doi: 10.1016/0092-8674(80)90425-0. [DOI] [PubMed] [Google Scholar]
  3. Bauer C., Tamm R., Petschow D., Bartels R., Bartels H. Oxygen affinity and allosteric effects of embryonic mouse haemolglobins. Nature. 1975 Sep 25;257(5524):333–334. doi: 10.1038/257333a0. [DOI] [PubMed] [Google Scholar]
  4. Brimhall B., Vedvick T. S., Jones R. T., Ahern E., Palomino E., Ahern V. Haemoglobin F Port Royal (alpha2G gamma2 125 Glu leads to Ala). Br J Haematol. 1974 Jun;27(2):313–318. doi: 10.1111/j.1365-2141.1974.tb06798.x. [DOI] [PubMed] [Google Scholar]
  5. Campbell D. G., Gagnon J., Reid K. B., Williams A. F. Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region. Biochem J. 1981 Apr 1;195(1):15–30. doi: 10.1042/bj1950015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Capp G. L., Rigas D. A., Jones R. T. Evidence for a new haemoglobin chain (zeta-chain). Nature. 1970 Oct 17;228(5268):278–280. doi: 10.1038/228278b0. [DOI] [PubMed] [Google Scholar]
  7. Capp G. L., Rigas D. A., Jones R. T. Hemoglobin Portland 1: a new human hemoglobin unique in structure. Science. 1967 Jul 7;157(3784):65–66. doi: 10.1126/science.157.3784.65. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Clegg J. B., Naughton M. A., Weatherball D. J. Abnormal human haemoglobins. Separation and characterization of the alpha and beta chains by chromatography, and the determination of two new variants, hb Chesapeak and hb J (Bangkok). J Mol Biol. 1966 Aug;19(1):91–108. doi: 10.1016/s0022-2836(66)80052-9. [DOI] [PubMed] [Google Scholar]
  10. Deisseroth A., Nienhuis A., Turner P., Velez R., Anderson W. F., Ruddle F., Lawrence J., Creagan R., Kucherlapati R. Localization of the human alpha-globin structural gene to chromosome 16 in somatic cell hybrids by molecular hybridization assay. Cell. 1977 Sep;12(1):205–218. doi: 10.1016/0092-8674(77)90198-2. [DOI] [PubMed] [Google Scholar]
  11. Efstratiadis A., Posakony J. W., Maniatis T., Lawn R. M., O'Connell C., Spritz R. A., DeRiel J. K., Forget B. G., Weissman S. M., Slightom J. L. The structure and evolution of the human beta-globin gene family. Cell. 1980 Oct;21(3):653–668. doi: 10.1016/0092-8674(80)90429-8. [DOI] [PubMed] [Google Scholar]
  12. Gale R. E., Clegg J. B., Huehns E. R. Human embryonic haemoglobins Gower 1 and Gower 2. Nature. 1979 Jul 12;280(5718):162–164. doi: 10.1038/280162a0. [DOI] [PubMed] [Google Scholar]
  13. HUEHNS E. R., FLYNN F. V., BUTLER E. A., BEAVEN G. H. Two new haemoglobin variants in a very young human embryo. Nature. 1961 Feb 11;189:496–497. doi: 10.1038/189496a0. [DOI] [PubMed] [Google Scholar]
  14. Huehns E. R., Faroqui A. M. Oxygen dissociation properties of human embryonic red cells. Nature. 1975 Mar 27;254(5498):335–337. doi: 10.1038/254335a0. [DOI] [PubMed] [Google Scholar]
  15. Hunkapiller M. W., Hood L. E. Direct microsequence analysis of polypeptides using an improved sequenator, a nonprotein carrier (polybrene), and high pressure liquid chromatography. Biochemistry. 1978 May 30;17(11):2124–2133. doi: 10.1021/bi00604a016. [DOI] [PubMed] [Google Scholar]
  16. Jelkmann W., Bauer C. Embryonic hemoglobins: dependency of functional characteristics on tetramer composition. Pflugers Arch. 1978 Oct 18;377(1):75–80. doi: 10.1007/BF00584377. [DOI] [PubMed] [Google Scholar]
  17. Kaltsoya A., Fessas P., Stavropoulos A. Hemoglobins of early human embryonic development. Science. 1966 Sep 16;153(3742):1417–1418. doi: 10.1126/science.153.3742.1417. [DOI] [PubMed] [Google Scholar]
  18. Kamuzora H., Lehmann H. Human embryonic haemoglobins including a comparison by homology of the human beta and alpha chains. Nature. 1975 Aug 7;256(5517):511–513. doi: 10.1038/256511a0. [DOI] [PubMed] [Google Scholar]
  19. Kilmartin J. V. Interaction of haemoglobin with protons, CO2 and 2,3-diphosphoglycerate. Br Med Bull. 1976 Sep;32(3):209–212. doi: 10.1093/oxfordjournals.bmb.a071364. [DOI] [PubMed] [Google Scholar]
  20. Kitchen H., Brett I. Embryonic and fetal hemoglobin in animals. Ann N Y Acad Sci. 1974 Nov 29;241(0):653–671. doi: 10.1111/j.1749-6632.1974.tb21921.x. [DOI] [PubMed] [Google Scholar]
  21. Klapper D. G., Wilde C. E., 3rd, Capra J. D. Automated amino acid sequence of small peptides utilizing Polybrene. Anal Biochem. 1978 Mar;85(1):126–131. doi: 10.1016/0003-2697(78)90282-8. [DOI] [PubMed] [Google Scholar]
  22. Ladner R. C., Heidner E. J., Perutz M. F. The structure of horse methaemoglobin at 2-0 A resolution. J Mol Biol. 1977 Aug 15;114(3):385–414. doi: 10.1016/0022-2836(77)90256-x. [DOI] [PubMed] [Google Scholar]
  23. Lauer J., Shen C. K., Maniatis T. The chromosomal arrangement of human alpha-like globin genes: sequence homology and alpha-globin gene deletions. Cell. 1980 May;20(1):119–130. doi: 10.1016/0092-8674(80)90240-8. [DOI] [PubMed] [Google Scholar]
  24. Lawn R. M., Efstratiadis A., O'Connell C., Maniatis T. The nucleotide sequence of the human beta-globin gene. Cell. 1980 Oct;21(3):647–651. doi: 10.1016/0092-8674(80)90428-6. [DOI] [PubMed] [Google Scholar]
  25. Melderis H., Steinheider G., Ostertag W. Evidence for a unique kind of alpha-type globin chain in early mammalian embryos. Nature. 1974 Aug 30;250(5469):774–776. doi: 10.1038/250774a0. [DOI] [PubMed] [Google Scholar]
  26. Pressley L., Higgs D. R., Clegg J. B., Weatherall D. J. Gene deletions in alpha thalassemia prove that the 5' zeta locus is functional. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3586–3589. doi: 10.1073/pnas.77.6.3586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. SANGER F., THOMPSON E. O. Halogenation of tyrosine during acid hydrolysis. Biochim Biophys Acta. 1963 May 14;71:468–471. doi: 10.1016/0006-3002(63)91108-9. [DOI] [PubMed] [Google Scholar]
  28. Slightom J. L., Blechl A. E., Smithies O. Human fetal G gamma- and A gamma-globin genes: complete nucleotide sequences suggest that DNA can be exchanged between these duplicated genes. Cell. 1980 Oct;21(3):627–638. doi: 10.1016/0092-8674(80)90426-2. [DOI] [PubMed] [Google Scholar]
  29. Spritz R. A., DeRiel J. K., Forget B. G., Weissman S. M. Complete nucleotide sequence of the human delta-globin gene. Cell. 1980 Oct;21(3):639–646. doi: 10.1016/0092-8674(80)90427-4. [DOI] [PubMed] [Google Scholar]
  30. Terhorst C., Robb R., Jones C., Strominger J. L. Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins. Proc Natl Acad Sci U S A. 1977 Sep;74(9):4002–4006. doi: 10.1073/pnas.74.9.4002. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Tuchinda S., Nagai K., Lehmann H. Oxygen dissociation curve of haemoglobin Portland. FEBS Lett. 1975 Jan 1;49(3):390–391. doi: 10.1016/0014-5793(75)80792-7. [DOI] [PubMed] [Google Scholar]
  32. Zimmer E. A., Martin S. L., Beverley S. M., Kan Y. W., Wilson A. C. Rapid duplication and loss of genes coding for the alpha chains of hemoglobin. Proc Natl Acad Sci U S A. 1980 Apr;77(4):2158–2162. doi: 10.1073/pnas.77.4.2158. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES