Antigenic Properties of Human Erythrocyte Glycophorins

  • Elwira Lisowska
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 228)


The name of glycophorin was given by Marchesi et al. (1972) to the major sialoglycophorin of human erythrocyte membranes, known earlier as the glycoprotein carrying blood group M and N determinants and receptors for agglutinins of influenza viruses (Baranowski et al., 1959; Romanowska 1959; Klenk & Uhlenbruck, 1960; Kathan et al., 1961; Springer et al., 1966). Fractionation of the erythrocyte membranes by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and visualization of sialoglycoproteins with periodic acid-Schiff (PAS) reagent give a complex pattern of bands which may differ in details, depending on electro- phoretic conditions. It has been now accepted that there are at least four distinct sialoglycoproteins in human erythrocyte membranes. Furthmayr et al. (1975) designated three of them as glycophorin A, B and C, in order of their decreasing amount in the membrane. Anstee et al. (1979) denoted them glycoprotein α, β, γ and δ, in order of their decreasing molecular weight. Dahr et al. (1978c) used other designations. The more numerous bands seen in SDS-PAGE correspond to monomers of the sialoglycoproteins and to homo- and heterodimers (and higher oligomers) formed by the most abundant glycophorins A and B (Fig. 1).


Blood Group Human Erythrocyte Sialic Acid Residue Blood Group Antigen Oligosaccharide Chain 
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© Plenum Press, New York 1988

Authors and Affiliations

  • Elwira Lisowska
    • 1
  1. 1.Department of ImmunochemistryInstitute of Immunology and Experimental Therapy Polish Academy of SciencesPoland

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