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Structural analysis of a membrane glycoprotein: Glycophorin A
Journal of Supramolecular Structure, 1977AbstractGlycophorin A is the major sialoglycoprotein of the human erythrocyte membrane. Structural studies indicate that this molecule is made up of 3 domains composed of 2 hydrophilic segments which are separated by a region of 22 nonpolar amino acids.
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Antigenic Properties of Human Glycophorins - An Update
2001Glycophorins are complex heavily glycosylated antigens carrying peptidic and glycopeptidic epitopes. Detailed immunochemical studies showed that GPA/GPB and GPC/GPD molecules have defined sites which are particularly immunogenic. These sites include N-terminal portions of all glycophorins, internal fragments of their extracellular domains, and ...
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Antigenic Properties of Human Erythrocyte Glycophorins
1988The 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.,
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Structural stability of glycophorin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978David M. Byers, Jacob A. Verpoorte
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GLYCOPHORIN AS A POSSIBLE RECEPTOR FOR PLASMODIUM FALCIPARUM
Lancet, The, 1982S F Parsons +2 more
exaly
pH titration studies of 13C reductively methylated N-terminal serine of glycophorin AM
International Journal of Biological Macromolecules, 1984Kilian Dill, Robert E Hardy
exaly