The structure of glycophorins of animal erythrocytes |
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Authors: | Hubert Krotkiewski |
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Institution: | (1) Department of Immunochemistry, Ludwik Hirsfelld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, 53-114 Wroclaw, Poland;(2) Present address: Department of Carbohydrate Chemistry, University of Lund, S-22370 Lund, Sweden |
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Abstract: | Glycophorins are red cell membrane sialoglycoproteins, which contain multipleO-linked oligosacchride chains and carry most of the cell surface sialic acid. Due to this high content of sialic acid the glycophorins are strongly stained with periodic acid-Schiff (PAS) reagent after sodium sodicylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The term glycophorin was proposed initially for human red cell sialoglycoproteins 1,2] and now it is also used for sialoglycoproteins in animal red cell membranes. Furthermore, similar glycoproteins of non-erythrocyte origin have also been identified and given the same name 3], although the terms leukosialin and sialophorin were proposed for a major sialoglycoproteins of human leukocytes 4,5]. In this article the term glycophorin will be used only for sialoglycoproteins existing in the erythrocyte membrane.Glycophorins of human erythrocytes, carrying blood group MN, Ss and other determinants, have been thoroughly studied and their properties described in several review articles 3,6,7,8]. The aim of this article is to summarize studies carriedout on the structure of non-human glycophorins, although some data concerning human glycophorins are included for comparative purposes.Abbreviations SDS-PAGE
sodium dodecylsulphate-polycrylamide gel electrophoresis
- PAS
periodic acid-Schiff
- LIS
lithium diiodosalicylate |
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Keywords: | glycophorin carbohydrate structure |
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