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Reactions of Erythrocyte Glycoproteins and their Degradation Products with various Anti‐I Sera
Author(s) -
Lisowska Elwira,
DzierźkowaBorodej Wanda,
Seyfried Halina,
Drzeniek Zofia
Publication year - 1975
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1975.tb02750.x
Subject(s) - glycoprotein , sialoglycoprotein , oligosaccharide , chemistry , trypsin , biochemistry , erythrocyte membrane , sepharose , chromatography , digestion (alchemy) , membrane , enzyme
. 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‐I S and anti‐I D sera, and did not change or decreased the activity toward anti‐I F 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.