Linked Life Data

1599498

Source:http://linkedlifedata.com/resource/pubmed/id/1599498

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1992-7-8
pubmed:abstractText
Depending on metabolic conditions, xanthine oxidoreductase acts as either a dehydrogenase (XDH) or an oxidase (XOD). The metabolism of hypoxanthine and xanthine by the oxidase is associated with the production of reactive oxygen radicals. Reaction of reactive oxygen radicals with polyunsaturated fatty acids (lipid peroxidation) leads to the formation of malondialdehyde (MDA) and 4-hydroxynonenal (HNE), known to modify proteins by reaction with NH2- and SH-groups. Therefore, these aldehydes could influence both the activity of xanthine oxidoreductase and the XOD/XDH ratio. We found that incubation of xanthine oxidoreductase with MDA leads to an initial increase in XDH activity and to a continuous decrease in XOD activity, whereby the total activity decreases. This was in contrast to the effects of HNE which did not alter the XDH activity; XOD was however activated. This demonstrates that the lipid peroxidation products MDA and HNE are able to modify xanthine oxidoreductase similarly to a feed-back mechanism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2117-20
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
The influence of lipid peroxidation products (malondialdehyde, 4-hydroxynonenal) on xanthine oxidoreductase prepared from rat liver.
pubmed:affiliation
Institute of Pathological and Clinical Biochemistry, Charité, Humboldt-University of Berlin, Germany.
pubmed:publicationType
Journal Article