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 |
|---|---|
| Pages (from-to) | 779-791 |
| Number of pages | 13 |
| Journal | Molecular Immunology |
| Volume | 19 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jan 1 1982 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Molecular Biology
- Immunology
Cite this
Immunochemical studies of infectious mononucleosis-X. Characterization of a glycoprotein from horse erythrocytes which reacts with Paul-Bunnell antibody. / Caldwell, Karen E.; Cayer, Marilyn; Whitney, Philip L.; Fletcher, Mary Ann.
In: Molecular Immunology, Vol. 19, No. 6, 01.01.1982, p. 779-791.Research output: Contribution to journal › Article
}
TY - JOUR
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
PY - 1982/1/1
Y1 - 1982/1/1
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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UR - http://www.scopus.com/inward/citedby.url?scp=0020039510&partnerID=8YFLogxK
U2 - 10.1016/0161-5890(82)90004-9
DO - 10.1016/0161-5890(82)90004-9
M3 - Article
C2 - 6810102
AN - SCOPUS:0020039510
VL - 19
SP - 779
EP - 791
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 6
ER -