Reactions of Erythrocyte Glycoproteins and their Degradation Products with various Anti-I Sera |
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| Authors: | Elwira Lisowska Wanda Dzier&#;kowa-Borodej Halina Seyfried and Zofia Drzeniek |
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| Institution: | Department of Immunochemistry, Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, and Laboratory Department, District Blood Transfusion Centre, Wroclaw, and Department of Serology, Institute of Haematology, Warszawa |
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| Abstract: | Abstract. Three fractions of erythrocyte glycoproteins obtained from Sepharose 4-B chromatography were tested for I activity with ten serologically differentiated anti-I sera. The most active was fraction I, eluted at the void volume and containing the lowest amount of alkali-labile oligosaccharide chains. The desialization of glycoproteins increased their activity toward anti-IS and anti-ID sera, and did not change or decreased the activity toward anti-IF sera. The most abundant fraction II (major sialoglycoprotein of erythrocyte membranes) showed no or only a very weak I activity, but I-active glycopeptides were isolated from products of digestion of fraction II with trypsin. The major product of digestion, sialoglycopeptide IIT-2 showed I activity only after alkaline elimination of alkali-labile oligosaccharide chains. The results indicate that I receptors are present in hindered form on apparently I-inactive components of erythrocyte membrane. |
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