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 Å 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 × 105 lymphocytes was caused by 30 μg of glycoprotein.
Original language | English (US) |
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Pages (from-to) | 779-791 |
Number of pages | 13 |
Journal | Molecular Immunology |
Volume | 19 |
Issue number | 6 |
DOIs | |
State | Published - Jun 1982 |
ASJC Scopus subject areas
- Immunology
- Molecular Biology