Conformation-independent binding of monoglucosylated ribonuclease B to calnexin.
Cell
; 88(1): 29-38, 1997 Jan 10.
Article
en En
| MEDLINE
| ID: mdl-9019402
ABSTRACT
Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked glycoproteins in vivo. Using defined components, the binding of ribonuclease B (RNase B) Man7-Man9 glycoforms to the luminal domain of calnexin was observed in vitro only if RNase B was monoglucosylated. Binding was independent of the conformation of the glycoprotein. Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin. These observations directly demonstrate that calnexin can act exclusively as a lectin.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ribonucleasas
/
Proteínas de Unión al Calcio
Límite:
Animals
Idioma:
En
Revista:
Cell
Año:
1997
Tipo del documento:
Article
País de afiliación:
Canadá