Faculty Articles
Comparison of receptor properties of erythrocyte membrane glycoproteins
Publication Title
Developmental & Comparative Immunology
ISSN
0145305X
Publication Date
1-1-1982
Abstract
Membrane glycoproteins from horse, sheep, goat and bovine erythrocytes were solubilized and purified. These glycoproteins could be placed in three groups based on their degrees of glycosylation: The major bovine erythrocyte glycoprotein (BGII) had 77% sugar, the minor bovine glycoprotein (BGI) had 27% sugar and the others had approximately 50% sugar. Four of the glycoproteins aggregated in a uniform way in aqueous solution--one, BGII, did not. Four had similar subunit sizes of 25-34,000 daltons, but BGII was larger--55,000 daltons. Receptor functions (for plant and invertebrate lectins, antibodies and cell surfaces) of these glycoproteins were primarily those dependent upon the presence of terminal sialic acid residues.
Volume
6
Issue
4
First Page
765
Last Page
774
Disciplines
Medical Specialties | Medicine and Health Sciences | Osteopathic Medicine and Osteopathy
NSUWorks Citation
Klimas, Nancy G.; Caldwell, K. E.; Whitney, P. L.; and Fletcher, Mary A., "Comparison of receptor properties of erythrocyte membrane glycoproteins" (1982). Faculty Articles. 450.
https://nsuworks.nova.edu/hpd_com_faculty_articles/450