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Ultrastructure of a transmembrane glycoprotein, glycophorin A
Tissue and Cell, 1988The major sialoglycoprotein of the human red cell membrane, glycophorin A, was isolated and examined by rotary shadowing and transmission electron microscopy. The glycophorin A molecule appeared as a cloud-like structure with a short, dense core within a large cloud.
G E, Wise, L X, Oakford, J K, Dzandu
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1983
The major human red cell sialoglycoprotein, glycophorin A, is structurally one of the best known membrane proteins. Until recently, however, nothing was known about its biosynthesis. We found in 1979 that the K562 cell line is erythroid and synthesizes glycophorin A.
Odd Nygård, Peter Westermann
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The major human red cell sialoglycoprotein, glycophorin A, is structurally one of the best known membrane proteins. Until recently, however, nothing was known about its biosynthesis. We found in 1979 that the K562 cell line is erythroid and synthesizes glycophorin A.
Odd Nygård, Peter Westermann
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Differential splicing of the glycophorin A mRNA
ELECTROPHORESIS, 1994AbstractTwo truncated mRNAs, in contrast to the full length of mRNA associated with the glycophorin A gene (GpA‐TI, GpA‐TII), were isolated from erythroid cells cultured by the selective two‐phase liquid culture system for erythroid progenitors in peripheral blood from a normal individual.
T, Omi +4 more
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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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The Journal of Membrane Biology, 1984
Glycophorin A, a major glycoprotein of the erythrocyte membrane, has been incorporated into small unilamellar vesicles composed of a variety of pure and mixed phospholipids. Nuclear spin labels including 31P and 19F have been used at natural abundance or have been synthetically incorporated in lipids to act as probes of lipid-protein interaction ...
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Glycophorin A, a major glycoprotein of the erythrocyte membrane, has been incorporated into small unilamellar vesicles composed of a variety of pure and mixed phospholipids. Nuclear spin labels including 31P and 19F have been used at natural abundance or have been synthetically incorporated in lipids to act as probes of lipid-protein interaction ...
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[Glycophorin in forensic medicine].
Soudni lekarstvi, 2000Immunohistological evidence of glycophorin from paraffin sections of tissues fixed with formol, makes its possible to visualize membranes of preserved erythrocytes and fragments after their disintegration. This fact permits even after development of post-mortem changes to differentiate actual extravasation, manifested by a positive finding of ...
P, Klír +3 more
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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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