Immunochemical studies of infectious mononucleosis-X. Characterization of a glycoprotein from horse erythrocytes which reacts with Paul-Bunnell antibody

Karen E. Caldwell, Marilyn Cayer, Philip L. Whitney, Mary Ann Fletcher

Research output: Contribution to journalArticle

2 Scopus citations

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 languageEnglish (US)
Pages (from-to)779-791
Number of pages13
JournalMolecular Immunology
Volume19
Issue number6
DOIs
StatePublished - Jun 1982

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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