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Glycoproteins containing peanut-agglutinin receptors from human-peripheral-blood T-lymphocyte plasma membranes
A glycoprotein fraction possessing peanut agglutinin receptors has been isolated from detergent extracts of neuraminidase-treated human peripheral blood T-lymphocyte plasma membranes with affinity matrices comprising the peanut agglutinin co-valently immobilised on Sepharose 4B. This fraction could be specifically eluted from affinity columns using buffer solutions supplemented with 0.2 M D-galactose and was shown, by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (0.1%), to contain four major glycoprotein components with apparent molecular weights of 200000, 190000, 110000 and 95000. It is suggested, from the observed reactivity of these glycoproteins with various lectins in double-diffusion experiments, that they possess both O-glycosidically and N-glycosidically linked carbohydrates.
A glycoprotein fraction possessing peanut agglutinin receptors has been isolated from detergent extracts of neuraminidase-treated human peripheral blood T-lymphocyte plasma membranes with affinity matrices comprising the peanut agglutinin co-valently immobilised on Sepharose 4B. This fraction could be specifically eluted from affinity columns using buffer solutions supplemented with 0.2 M D-galactose and was shown, by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (0.1%), to contain four major glycoprotein components with apparent molecular weights of 200000, 190000, 110000 and 95000. It is suggested, from the observed reactivity of these glycoproteins with various lectins in double-diffusion experiments, that they possess both O-glycosidically and N-glycosidically linked carbohydrates.