Comparison of isolated peanut agglutinin receptor glycoproteins from human, bovine and porcine erythrocyte membranes.

Affinity chromtography has been used to isolate and compare the peanut agglutinin receptors from neuraminidase-treated human, bovine and porcine erythrocyte membranes. Passage of Triton X-100-solubilised membrane material through either Sepharose- or acrylamide-based affinity columns resulted in the reversible binding of receptor molecules to the immobilised lectin. Elution with 0.2 M galactose released specifically bound glycoprotein fractions, the composition and molecular weights of which were determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. Carbohydrate analysis by gas chromatography identified these bound glycoprotein fractions as the major sources of the O-glycosidic-linked disaccharide galactosyl-beta-(1 leads to 3)-N-acetylgalactosamine in these membranes. It is suggested that these isolated fractions represent a discrete population of glycoproteins within the membranes studied, which possess both O-glycosidic- and N-glycosidic-linked carbohydrates.