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

doi:10.1016/0161-5890(82)90004-9

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	779-791
Number of pages	13
Journal	Molecular Immunology
Volume	19
Issue number	6
DOIs	https://doi.org/10.1016/0161-5890(82)90004-9
State	Published - Jun 1982
Externally published	Yes

ASJC Scopus subject areas

Immunology
Molecular Biology

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10.1016/0161-5890(82)90004-9

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

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 {\AA} 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.",

author = "Caldwell, {Karen E.} and Marilyn Cayer and Whitney, {Philip L.} and Fletcher, {Mary Ann}",

note = "Funding Information: *Supported by NIH grant AM16763. tTo whom correspondence should be addressed.",

year = "1982",

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T1 - Immunochemical studies of infectious mononucleosis-X. Characterization of a glycoprotein from horse erythrocytes which reacts with Paul-Bunnell antibody

AU - Caldwell, Karen E.

AU - Cayer, Marilyn

AU - Whitney, Philip L.

AU - Fletcher, Mary Ann

N1 - Funding Information: *Supported by NIH grant AM16763. tTo whom correspondence should be addressed.

PY - 1982/6

Y1 - 1982/6

N2 - 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.

AB - 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.

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

Abstract

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