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- W2108542943 abstract "The 2 types of erythrocytes from a person with persistent mixed-field polyagglutinability (Tn abnormality) were separated from each other by preparative cell electrophoresis. Surface labelling using the galactose oxidase/NaB3H4 technique followed by polyacrylamide gel electrophoresis showed a strong labelling in the glycophorin A region of Tn positive erythrocytes indicating exposed galactosyl N-acetyl/galactosaminyl residues. Tn positive cell membranes were labelled by the galactose oxidase/NaB3H4 technique and solubilized in non-ionic detergent. After chromatography on Helix pomatia lectin-linked Sepharose, glycophorin A was immunoprecipitated from the sugar eluate using specific antiserum. Glycophorin A from Tn negative cells and normal red blood cells did not bind to Helix pomatia lectin but to Lens culinaris lectin-Sepharose. Glycophorin A and band 3 were isolated by preparative gel electrophoresis from normal cells and the two red cell populations of the Tn individual. Pronase treatment of labelled glycophorin A followed by gel filtration revealed a more efficient proteolysis in molecules isolated from Tn positive cells. Mild alkaline treatment of galactose oxidase/NaB3H4 or periodate/NaB3H4 labelled glycophorin A liberated 3 different oligosaccharides from Tn positive cells. No significant difference was found between the oligosaccharides of band 3 protein from normal and Tn positive cells and the amounts of glycophorin A were identical in both cell types when determined by radioimmunoassay." @default.
- W2108542943 created "2016-06-24" @default.
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- W2108542943 date "2009-04-24" @default.
- W2108542943 modified "2023-09-27" @default.
- W2108542943 title "Characterization of Glycophorin A and Band 3 from Tn Polyagglutinable Erythrocytes" @default.
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- W2108542943 doi "https://doi.org/10.1111/j.1600-0609.1981.tb01659.x" @default.
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