Glucosylation of membrane-bound proteins by lipid-linked glucose.
Planta
; 140(2): 177-83, 1978 Jan.
Article
em En
| MEDLINE
| ID: mdl-24414475
ABSTRACT
Particulate preparations from Pisum sativum. were able to incorporate [(14)C]glucose from UDP-[(14)C]glucose into oligosaccharide-linked lipids was formed by an oligosaccharide chain containing 7-8 glucose residues linked to dolichol, presumably via a pyrophosphate. The polymer was identified as a membrane-bound glucoprotein that could be solubilized by Triton X-100. SDS gel electrophoresis showed that a polypeptide with an apparent molecular weight of 13,000 could be glucosylated from dolichyl-phosphate-glucose. This was coincident with the electrophoretic mobility of the ß subunit of the pea lectin in the same system. The glucosylated protein was solubilized from the membranes by sonication and showed the same carbohydrate-binding ability as pea lectins. These results strongly suggest that pea lectins can be glucosylated by the lipid intermediate pathway.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
Planta
Ano de publicação:
1978
Tipo de documento:
Article
País de afiliação:
Argentina