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. 1976 Jun 1;155(3):701–703. doi: 10.1042/bj1550701

Abnormal carbohydrate composition of the major penetrating membrane protein of En(a-) human erythrocytes.

M J Tanner, R E Jenkins, D J Anstee, J R Clamp
PMCID: PMC1172895  PMID: 949329

Abstract

The major penetrating membrane glycoprotein (band 3) was isolated from En(a-) and normal human erythrocytes. The two proteins differed only in carbohydrate composition. Band 3 from En(a-) erythrocytes contained greater amounts of galactose and N-acetyl-glucosamine. The loss of the sialoglycoprotein sialotetrasaccharides in the En(a-) cell is not compensated by the appearance of these units in band 3 of En(a-) erythrocytes.

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Selected References

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  1. Boxer D. H., Jenkins R. E., Tanner M. J. The organization of the major protein of the human erythrocyte membrane. Biochem J. 1974 Mar;137(3):531–534. doi: 10.1042/bj1370531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bretscher M. S. Membrane structure: some general principles. Science. 1973 Aug 17;181(4100):622–629. doi: 10.1126/science.181.4100.622. [DOI] [PubMed] [Google Scholar]
  3. Cabantchik Z. I., Rothstein A. Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation. J Membr Biol. 1974;15(3):207–226. doi: 10.1007/BF01870088. [DOI] [PubMed] [Google Scholar]
  4. Clamp J. R. Analysis of glycoproteins. Biochem Soc Symp. 1974;(40):3–16. [PubMed] [Google Scholar]
  5. Dahr W., Uhlenbruck G., Bird G. W. Further characterization of some heterophile agglutinins reacting with alkali-labile carbohydrate chains of human erythrocyte glycoproteins. Vox Sang. 1975;28(2):133–148. doi: 10.1111/j.1423-0410.1975.tb02751.x. [DOI] [PubMed] [Google Scholar]
  6. Furuhjelm U., Nevanlinna H. R., Pirkola A. A second Finnish En(a-) propositus with anti-Ena. Vox Sang. 1973;24(6):545–549. doi: 10.1111/j.1423-0410.1973.tb03498.x. [DOI] [PubMed] [Google Scholar]
  7. Halestrap A. P. Transport of pyruvate nad lactate into human erythrocytes. Evidence for the involvement of the chloride carrier and a chloride-independent carrier. Biochem J. 1976 May 15;156(2):193–207. doi: 10.1042/bj1560193. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. McFarlane A. S. IN VIVO BEHAVIOR OF I-FIBRINOGEN. J Clin Invest. 1963 Mar;42(3):346–361. doi: 10.1172/JCI104721. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Roseman S. The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion. Chem Phys Lipids. 1970 Oct;5(1):270–297. doi: 10.1016/0009-3084(70)90024-1. [DOI] [PubMed] [Google Scholar]
  11. Steck T. L. The organization of proteins in the human red blood cell membrane. A review. J Cell Biol. 1974 Jul;62(1):1–19. doi: 10.1083/jcb.62.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Tanner M. J., Anstee D. J. The membrane change in En(a-) human erythrocytes. Absence of the major erythrocyte sialoglycoprotein. Biochem J. 1976 Feb 1;153(2):271–277. doi: 10.1042/bj1530271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Tanner M. J., Boxer D. H. Separation and some properties of the major proteins of the human erythrocyte membrane. Biochem J. 1972 Sep;129(2):333–347. doi: 10.1042/bj1290333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Thomas D. B., Winzler R. J. Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides. J Biol Chem. 1969 Nov 10;244(21):5943–5946. [PubMed] [Google Scholar]
  15. Tomita M., Marchesi V. T. Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2964–2968. doi: 10.1073/pnas.72.8.2964. [DOI] [PMC free article] [PubMed] [Google Scholar]

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