Faculty Articles
Title
Comparison of receptor properties of erythrocyte membrane glycoproteins
ISBN or ISSN
0145305X
Publication Title
Developmental & Comparative Immunology
Volume
6
Issue
4
Publication Date / Copyright Date
1-1-1982
First Page
765
Last Page
774
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.
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
