title: Glucosylation of membrane-bound proteins by lipid-linked glucose.
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 β 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.
authors.affiliation: Departamento de Biología, Fundación Bariloche, Casilla de Correo 138, 8400, San Carlos de Bariloche, Argentina.
authors.forename: R
authors.initials: R
authors.lastname: Pont Lezica
authors.forename: P A
authors.initials: PA
authors.lastname: Romero
authors.forename: H E
authors.initials: HE
authors.lastname: Hopp