Crosslinking of the Glycoproteins in Human Erythrocyte Membranes
AUTOR(ES)
Ji, T. H.
RESUMO
The glycoproteins of human erythrocyte membranes were crosslinked with dimethyl adipimidate dihydrochloride. On sodium dodecyl sulfate-polyacrylamide gel electrophoregrams of the crosslinked solubilized membranes, at least three new glycoprotein complexes appeared in addition to the normal glycoprotein species. One of the new glycoprotein complexes was shown to contain two of the three species of membrane glycoproteins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=387939Documentos Relacionados
- STUDIES OF THE METABOLISM OF HUMAN ERYTHROCYTE MEMBRANES*
- Proteinase-resistant factors in human erythrocyte membranes mediate CD4-dependent fusion with cells expressing human immunodeficiency virus type 1 envelope glycoproteins.
- Solubilization of human erythrocyte membranes by ASB detergents
- Glycosyltransferases in human blood: I. Galactosyltransferase in human serum and erythrocyte membranes
- Identification of high affinity folate binding proteins in human erythrocyte membranes.