About: Modification of simian virus 40 large tumor antigen by glycosylation

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Modification of simian virus 40 large tumor antigen by glycosylation Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Modification of simian virus 40 large tumor antigen by glycosylation
Creator	Jarvis, Donald Butel', Janet
source	Elsevier; Medline; PMC
abstract	Abstract The SV40-encoded transforming protein, large tumor antigen (T-ag), is multifunctional. Chemical modifications of the T-ag polypeptide may be important for its multifunctional capacity. T-ag is additionally modified by glycosylation. T-ag was metabolically labeled in SV40-infected cells with tritiated galactose or glucosamine, but not with mannose or fucose. The identity of glycosylated T-ag was established by immunoprecipitation with a variety of T-ag-specific antisera, including monoclonal antibodies. Incorporation of labeled sugar into T-ag was inhibited in the presence of excess unlabeled sugars, but not in the presence of excess unlabeled amino acids. Labeled monosaccharides could be preferentially removed from T-ag with a mixture of glycosidic enzymes. In addition, galactose was removed from purified T-ag by acid hydrolysis and identified as such by thin-layer chromatography. T-ag oligosaccharides were resistant to treatment with EndoH, and glycosylation was not inhibited by tunicamycin. Together, these data strongly suggest that T-ag is glycosylated. Several characteristics, including lack of mannose labeling, EndoH resistance, and tunicamycin resistance, suggest that T-ag is not an N-linked glycoprotein. Rather, these properties are more consistent with the identification of T-ag as an O-linked glycoprotein.
has issue date	1985-03-31(xsd:dateTime)
bibo:doi	10.1016/0042-6822(85)90250-8
bibo:pmid	3002015
has license	els-covid
sha1sum (hex)	2bb60c5dc8bdb5328cfb611ae328786e9e76433b
schema:url	https://doi.org/10.1016/0042-6822%2885%2990250-8
resource representing a document's title	Modification of simian virus 40 large tumor antigen by glycosylation
has PubMed Central identifier	PMC7130735
has PubMed identifier	3002015
schema:publication	Virology
resource representing a document's body	covid:2bb60c5dc8bdb5328cfb611ae328786e9e76433b#body_text
is schema:about of	named entity 'LARGE TUMOR ANTIGEN' named entity 'GLYCOSYLATION' named entity 'SIMIAN VIRUS 40' named entity 'MODIFICATION' named entity 'Simian Virus 40' named entity 'T-ag' named entity 'N-glycosylated' named entity 'protein' named entity 'commer' named entity 'glucose' named entity 'starvation' named entity 'T-ag' named entity 'TBS' named entity 'Immunoprecipitates' named entity 'sugar' named entity 'fucose' named entity 'T-ag' named entity 'methionine' named entity 'SDS-PAGE' named entity 'immunoprecipitated' named entity 'small tumor antigen' named entity 'amino acids' named entity 'T-ag' named entity 'SV40' named entity 'sugar' named entity 'galactose' named entity 'methionine' named entity 'glucose' named entity 'glycosylation' named entity 'Molecular weight' named entity 'thin-layer chromatography' named entity 'isotope' named entity 'T-ag' named entity 'NaCl' named entity 'oligosaccharides' named entity 'Glucose' named entity 'T-ag' named entity 'sugar' named entity 'macromolecules' named entity 'Miles Laboratories, Inc.' named entity 'glycosylation' named entity 'galactose' named entity 'TBS' named entity 'polypeptide' named entity 'glycoprotein' named entity 'hydrolysate' named entity 'T-ag' named entity 'T-ag' named entity 'ribose' named entity 'New York' named entity 'staining' named entity 'glycosylated' named entity 'T-ag' named entity 'galactose' named entity 'N-linked' named entity 'T-ag' named entity 'covalent' named entity 'amino acid residues' named entity 'chemical modifications' named entity 'antigenic determinants' named entity 'Takatsuki' named entity 'galactose' named entity 'polypeptide' named entity 'monosaccharides' named entity 'N. J.' named entity 'tunicamycin' named entity 'multiplicity of infection' named entity 'spectroscopy' named entity 'TCA' named entity 'IgG' named entity 'immune complexes' named entity 'eluted' named entity 'DNA-binding' named entity 'T-ag' named entity 'galactose' named entity 'T-ag' named entity 'VSV' named entity 'Ile' named entity 'antigens' named entity 'oligonucleotides'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software