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. 1976 Aug 15;158(2):497–500. doi: 10.1042/bj1580497

Identification of a sialoglycopeptide released by self-digestion from human erythrocyte membranes.

A Brovelli, G Pallavicini, F Sinigaglia, C L Balduini, C Balduini
PMCID: PMC1163996  PMID: 985443

Abstract

Membranes from human O Rhesus-positive erythrocyte 'ghosts' were tested in vitro for their ability to digest their own glycoproteins. 'Ghost' membranes incubated in Tris/HCl buffer, pH 7.4, release a sialoglycopeptide, which contains glucosamine, galactosamine, galactose and mainly polar amino acids. Chemical composition, molecular size and aggregation properties suggest that this glycopeptide may be a fragment of glycophorin.

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Selected References

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

  1. Balduini C., Balduini C. L., Ascari E. Membrane glycopeptides from old and young human erythrocytes. Biochem J. 1974 Jun;140(3):557–560. doi: 10.1042/bj1400557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baxter A., Beeley J. G. Changes in surface carbohydrate of human erythrocytes aged in vivo. Biochem Soc Trans. 1975;3(1):134–136. doi: 10.1042/bst0030134. [DOI] [PubMed] [Google Scholar]
  3. COOK G. M., EYLAR E. H. SEPARATION OF THE M AND N BLOOD-GROUP ANTIGENS OF THE HUMAN ERYTHROCYTE. Biochim Biophys Acta. 1965 Mar 1;101:57–66. doi: 10.1016/0926-6534(65)90030-8. [DOI] [PubMed] [Google Scholar]
  4. Cetta G., Pallavicini G., Calatroni A., Castellani A. A. Glycoproteins from bovine duodenal mucosa. Ital J Biochem. 1972 Sep-Dec;21(5):275–288. [PubMed] [Google Scholar]
  5. Durocher J. R., Payne R. C., Conrad M. E. Role of sialic acid in erythrocyte survival. Blood. 1975 Jan;45(1):11–20. [PubMed] [Google Scholar]
  6. EYLAR E. H., MADOFF M. A., BRODY O. V., ONCLEY J. L. The contribution of sialic acid to the surface charge of the erythrocyte. J Biol Chem. 1962 Jun;237:1992–2000. [PubMed] [Google Scholar]
  7. Ebert W., Metz J., Roelcke D. Modifications of N-acetylneuraminic acid and their influence on the antigen activity of erythrocyte glycoproteins. Eur J Biochem. 1972 Jun 9;27(3):470–472. doi: 10.1111/j.1432-1033.1972.tb01862.x. [DOI] [PubMed] [Google Scholar]
  8. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  9. Gattegno L., Bladier D., Cornillot P. Ageing in vivo and neuraminidase treatment of rabbit erythrocytes: influence on half-life as assessed by 51Cr labelling. Hoppe Seylers Z Physiol Chem. 1975 Apr;356(4):391–397. doi: 10.1515/bchm2.1975.356.1.391. [DOI] [PubMed] [Google Scholar]
  10. Guidotti G. Membrane proteins. Annu Rev Biochem. 1972;41:731–752. doi: 10.1146/annurev.bi.41.070172.003503. [DOI] [PubMed] [Google Scholar]
  11. Hughes R. C. Glycoproteins as components of cellular membranes. Prog Biophys Mol Biol. 1973;26:189–268. doi: 10.1016/0079-6107(73)90020-5. [DOI] [PubMed] [Google Scholar]
  12. Janado M. Analysis of a reversibly polymerizing system by frontal gel filtration. Aggregation of a human erythrocyte membrane glycoprotein. J Biochem. 1974 Dec;76(6):1183–1189. doi: 10.1093/oxfordjournals.jbchem.a130671. [DOI] [PubMed] [Google Scholar]
  13. Janado M., Azuma J., Onodera K. Reversible aggregation of a human erythrocyte membrane glycoprotein. J Biochem. 1973 Nov;74(5):881–887. [PubMed] [Google Scholar]
  14. Jancik J., Schauer R. Sialic acid--a determinant of the life-time of rabbit erythrocytes. Hoppe Seylers Z Physiol Chem. 1974 Apr;355(4):395–400. doi: 10.1515/bchm2.1974.355.1.395. [DOI] [PubMed] [Google Scholar]
  15. MOORE S., STEIN W. H. Chromatography of amino acids on sulfonated polystyrene resins. J Biol Chem. 1951 Oct;192(2):663–681. [PubMed] [Google Scholar]
  16. MORRISON W. L., NEURATH H. Proteolytic enzymes of the formed elements of human blood. I. Erythrocytes. J Biol Chem. 1953 Jan;200(1):39–51. [PubMed] [Google Scholar]
  17. Marchesi V. T., Jackson R. L., Segrest J. P., Kahane I. Molecular features of the major glycoprotein of the human erythrocyte membrane. Fed Proc. 1973 Aug;32(8):1833–1837. [PubMed] [Google Scholar]
  18. Marchesi V. T., Palade G. E. The localization of Mg-Na-K-activated adenosine triphosphatase on red cell ghost membranes. J Cell Biol. 1967 Nov;35(2):385–404. doi: 10.1083/jcb.35.2.385. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Marchesi V. T., Tillack T. W., Jackson R. L., Segrest J. P., Scott R. E. Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1445–1449. doi: 10.1073/pnas.69.6.1445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Moore G. L., Kocholaty W. F., Cooper D. A., Gray J. L., Robinson S. L. A proteinase from human erythrocyte membranes. Biochim Biophys Acta. 1970 Jul 15;212(1):126–133. doi: 10.1016/0005-2744(70)90185-3. [DOI] [PubMed] [Google Scholar]
  21. Springer G. F., Nagai Y., Tegtmeyer H. Isolation and properties of human blood-group NN and meconium-Vg antigens. Biochemistry. 1966 Oct;5(10):3254–3272. doi: 10.1021/bi00874a028. [DOI] [PubMed] [Google Scholar]
  22. Tökés Z. A., Chambers S. M. Proteolytic activity associated with human erythrocyte membranes. Self-digestion of isolated human erythrocyte membranes. Biochim Biophys Acta. 1975 May 6;389(2):325–338. doi: 10.1016/0005-2736(75)90325-9. [DOI] [PubMed] [Google Scholar]
  23. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]

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