Glucosylation of membrane-bound proteins by lipid-linked glucose |
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Authors: | R Pont Lezica P A Romero H E Hopp |
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Institution: | (1) Departamento de Biología, Fundación Bariloche, Casilla de Correo 138, 8400 San Carlos de Bariloche, Argentina;(2) Biologie, Universität Kaiserslautern, Postfach 3049, D 6750 Kaiserslautern, Federal Republic of Germany;(3) Present address: Universidad Católica de Valparaiso, Chile;(4) Present address: Instituto de Investigaciones en Ciencias Agronómicas, INTA, C.C. 25 Castelar, Argentina;(5) Fundación Campomar, Instituto de Investigaciones Bioquímicas, Obligado 2490, 1428 Buenos Aires, Argentina |
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Abstract: | Particulate preparations from Pisum sativum. were able to incorporate 14C]glucose from UDP-14C]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 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.Abbreviations BSA
Bovine serum albumin
- Dol
dolichol
- SDS
sodium dodecyl sulfate |
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Keywords: | Lectins Pisum Polyprenyl-sugars Protein glucosylation |
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