Linked Life Data

20616208

Source:http://linkedlifedata.com/resource/pubmed/id/20616208

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-9-17
pubmed:abstractText
Free radicals generated during peroxidase-catalyzed oxidation of two xenobiotics, carcinogenic Sudan I and an anticancer agent ellipticine, easily attack unmodified proteins but not glycoproteins. A significant inverse correlation between the extent of glycosylation of proteins and the degree of binding of Sudan I or ellipticine radicals to these proteins was observed, whereby the protection only occurs if oligosaccharides are covalently bound to the proteins. No influence of any other variables was found and further confirmed by experiments with proteins containing identical polypeptide chains differing only by the absence (ribonuclease A) or the presence (ribonuclease B) of a single oligosaccharide. The free radicals that are subject of this study did not react with the oligosaccharides because higher levels of the corresponding dimers, reaction products of the radicals, were found in presence of highly glycosylated proteins. The results indicate that carbohydrates protect polypeptides against modification by free radicals derived from toxic xenobiotics and provide passive shielding of the protein moiety.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1096-0929
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
359-74
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Glycosylation protects proteins against free radicals generated from toxic xenobiotics.
pubmed:affiliation
Department of Biochemistry, Faculty of Science, Charles University Prague, 12840 Prague 2, Czech Republic.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't