Abstract
Early studies on the analysis of membranes isolated from the erythrocytes of Tn-patients by SDS-polyacrylamide gel elec-trophoresis (SDS-PAGE) revealed a severe reduction in the staining capacity of glycophorin with the periodate-Schiff (PAS) reaction1,2. A low sialic acid and galactose (Gal) content of the polyagglutinable red cells was confirmed3 while it was, reported2,4 that the abnormal red cells of Tn-patients contained little or no UDPGal: GalNAc-β-3-D-galactosyltransferase (T-transferase) activity. The glycoprotein (GP) abnormality in Tn-erythrocytes appeared to be due to incomplete synthesis of the alkali-labile oligosaccharide chains of glycophorin2. We now report studies on the membrane GP composition and the T-transferase activity of platelets isolated from three Tn-syndrome patients whose red cell membranes contain GP abnormalities which are typical of those found in this rare clinical condition1,2.
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Cartron, J., Nurden, A. Galactosyltransferase and membrane glycoprotein abnormality in human platelets from Tn-syndrome donors. Nature 282, 621–623 (1979). https://doi.org/10.1038/282621a0
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DOI: https://doi.org/10.1038/282621a0
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