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- W2020152240 abstract "A highly purified preparation of horse erythrocyte glycoprotein was prepared from an aqueous ethanolic extract of hemoglobin-free membranes. The subunit apparent mol. wt was 30,000. In aqueous solution the glycoprotein formed globular aggregates of 93 +/- 16 A diameter. The glycoprotein had a receptor for the Paul-Bunnell antibody of infectious mononucleosis which was associated with an O-glycosidically linked oligosaccharide and dependent on the presence of N-glycolylneuraminic acid. In addition the glycoprotein had a neuraminidase-sensitive receptor for human peripheral blood lymphocytes. Fifty per cent inhibition of the rosetting of sheep red cells by 4 x 10(5) lymphocytes was caused by 30 microgram of glycoprotein." @default.
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- W2020152240 date "1982-06-01" @default.
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- W2020152240 title "Immunochemical studies of infectious mononucleosis—X. Characterization of a glycoprotein from horse erythrocytes which reacts with Paul-Bunnell antibody" @default.
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- W2020152240 doi "https://doi.org/10.1016/0161-5890(82)90004-9" @default.
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