Linked Life Data

8374038

Source:http://linkedlifedata.com/resource/pubmed/id/8374038

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-10-18
pubmed:abstractText
An immunochemical assay was developed to detect carbonyl moieties that result from oxidative damage to proteins. Bovine serum albumin was reacted with hydroxyl radicals generated via a Fenton-like mechanism or by a radiolysis mechanism. The resulting albumin-derived carbonyls were reacted with 2,4-dinitrophenylhydrazine, giving the corresponding hydrazones, which were detected by Western blot using anti-dinitrophenyl antisera. The immunoblot demonstrated a concentration-dependent increase in carbonyl formation, as well as fragmentation of the albumin into two distinct bands with molecular masses of 51 and 45 kDa when oxidized with the Fenton-like mechanism, and 62 and 46 kDa when oxidized by radiolysis. Analysis of the immunoblot using laser densitometry indicated a linear relationship between carbonyl groups and increasing treatment from radiolysis. This immunochemical assay was approximately 3 orders of magnitude more sensitive than the spectrophotometric method and was able to determine the molecular mass of carbonyl-modified polypeptides in the detection of oxidative damage.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0893-228X
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
430-3
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Immunochemical detection of oxidized proteins.
pubmed:affiliation
Occupational and Environmental Health Program, University of Arkansas for Medical Sciences, Little Rock 72205-7199.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.