Abstract
Glycophorin A (GpA), which is the major sialoglycoprotein on human red cells, is one of the best characterized mammalian integral membrane proteins (Marchesi et al. 1972; Tomita and Marchesi 1975). Its amino acid sequence is known. The protein molecule contains three distinct domains. A large hydrophilic portion, carrying the NH2-terminal, is located on the external surface of the red cell, and the COOH-terminal is located in the cytoplasm (Bretscher 1975) and probably interacts with peripheral proteins on the inner aspect of the membrane. These two hydrophilic sequences are connected by a hydrophobic segment of 23 amino acids which must be embedded within the lipid bilayer.
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Andersson, L.C., von Willebrand, E., Jokinen, M., Karhi, K.K., Gahmberg, C.G. (1981). Glycophorin A as an Erythroid Marker in Normal and Malignant Hematopoiesis. In: Neth, R., Gallo, R.C., Graf, T., Mannweiler, K., Winkler, K. (eds) Modern Trends in Human Leukemia IV. Haematology and Blood Transfusion / Hämatologie und Bluttransfusion, vol 26. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67984-1_60
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DOI: https://doi.org/10.1007/978-3-642-67984-1_60
Publisher Name: Springer, Berlin, Heidelberg
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