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- W2033103439 abstract "Wheat germ agglutinin inhibited the agglutination of paraformaldehyde-fixed washed human platelets which is induced by ristocetin in the presence of plasma von Willebrand factor, a component of the factor VIII system. Affinity columns of wheat germ agglutinin in Sepharose 4B were used to isolate the surface glycoprotein I complex from detergent solubilized human platelet membranes. Two glycoproteins of Mr 150, 000 and Mr 210, 000 were eluted from the wheat germ column using N-acetyl glucosamine. This mixture of isolated surface glycoproteins blocked ristocetin-induced agglutination of fixed washed platelets. F(ab′)2 fragments of an antiserum raised to the eluted glycoprotein mixture inhibited ristocetin-induced platelet agglutination. By solid phase immunoabsorption, it was shown that the antibody which blocked the ristocetin reaction interacted with a platelet membrane protein of Mr 150, 000. The results suggest that the glycoprotein I complex on the surface of the human platelet mediates von Willebrand factor dependent ristocetin-induced platelet agglutination." @default.
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- W2033103439 date "1978-01-01" @default.
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- W2033103439 title "Wheat germ agglutinin affinity chromatography of human platelet membrane glycoproteins" @default.
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- W2033103439 doi "https://doi.org/10.1016/0049-3848(78)90088-9" @default.
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