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Open AccessJournal ArticleDOI

The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein.

E. Li, +2 more
- 10 Nov 1978 - 
- Vol. 253, Iss: 21, pp 7762-7770
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TLDR
The synthesis of the complex-type oligosaccharide unit of the vesicular stomatitis virus G protein is initiated by the en bloc transfer of a high molecular weight oligosACcharide from a lipid carrier to the nascent polypeptide.
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This article is published in Journal of Biological Chemistry.The article was published on 1978-11-10 and is currently open access. It has received 398 citations till now. The article focuses on the topics: Oligosaccharide & Mannose.

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Book ChapterDOI

Chapter 4 Membrane glycoproteins and glycolipids: structure, localization and function of the carbohydrate

TL;DR: This chapter describes the structure and localization of the carbohydrate portions of membrane glycoproteins and glycolipids and their relationships to functions.
Journal ArticleDOI

Altered synthesis and processing of oligosaccharides of vesicular stomatitis virus glycoprotein in different lectin-resistant Chinese hamster ovary cell lines.

L A Hunt
- 01 Aug 1980 - 
TL;DR: The results demonstrated that a double-mutant cell line selected from the phytohemagglutinin-resistant cells for resistance to concanavalin A had an additional defect in one of the earliest stages of glycosylation, resulting in smaller precursor oligosaccharides linked to protein.
Journal ArticleDOI

A UDP-glucose:glycoprotein glucose-1-phosphotransferase in embryonic chicken neural retina

TL;DR: It is proposed that GlcPTase may be a controlling enzyme for the targeting of certain newly synthesized proteins to the cell surface with a cation-exchange profile similar to that of oligosaccharides derived from ligatin-associated proteins synthesized in vivo.
Journal ArticleDOI

Formation of lipid-linked oligosaccharides by MOPC 315 plasmacytoma cells. Decreased synthesis by a nonsecretory variant.

TL;DR: If nucleotide pyrophosphatase is important for the control of substrates for glycosylation, it must regulate nucleotide sugar levels at a site other than the cytoplasm of cells, perhaps at the location of synthesis of the larger lipid-linked oligosaccharides.
Journal ArticleDOI

Cell-free synthesis and processing of the precursors to the subunits of luteinizing hormone.

TL;DR: Polyadenylated RNA prepared from pituitary glands of ovariectomized rats was translated in heterologous cell-free systems derived from wheat germ and rabbit reticulocytes in the absence and in the presence of pancreatic microsomal membranes to confirm the immunological identity of the glycosylated subunits of luteinizing hormone.
References
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Journal ArticleDOI

Detection of sugars on paper chromatograms.

W E Trevelyan, +2 more
- 09 Sep 1950 - 
TL;DR: Modifications are introduced, based on a test given by Feigl for reducing sugars, which eliminate the heating step, and in which the reagents are applied in organic solvents, thus removing the danger of migration of the sugar spots.
Journal ArticleDOI

Determination of aminosugar linkages in glycolipids by methylation: Aminosugar linkages of ceramide pentasaccharides of rabbit erythrocytes and of Forssman antigen☆

TL;DR: This method was successfully applied to analysis of aminosugar linkages in blood group B-active ceramide pentasaccharide from rabbit erythrocytes and in Forssman antigen of equine spleen.
Journal ArticleDOI

The role of polyprenol-linked sugars in glycoprotein synthesis.

TL;DR: The chiral stationary phase for lipid-Linked Monosaccharides showed good chiral recognition ability towards various lipids, and this property has been generalized to other lipids as well.
Journal ArticleDOI

Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity.

TL;DR: The presence of the unsubstituted alpha-mannosyl residue linked at the C-3 position of the terminal mannose of Manbeta1 leads to 4 GlcNAcAsn core must be essential for the action of the enzyme.
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