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  • Title: Immunochemical studies of infectious mononucleosis--X. Characterization of a glycoprotein from horse erythrocytes which reacts with Paul-Bunnell antibody.
    Author: Caldwell KE, Cayer M, Whitney PL, Fletcher MA.
    Journal: Mol Immunol; 1982 Jun; 19(6):779-91. PubMed ID: 6810102.
    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.
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