Linked Life Data

2275385

Source:http://linkedlifedata.com/resource/pubmed/id/2275385

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-2-28
pubmed:abstractText
In our preliminary study, it has been found that VX oxidase exists in the microsome fraction of rat liver and the catalytic reaction needs the participation of molecular oxygen and coenzyme I or II. In this paper, the data showed that deoxycholate inactivated both the mixed function oxidase and VX oxidase. The specific inhibitor proadifen of the mixed function oxidase also profoundly inhibited VX oxidase activity. The complex of VX and cytochrome P-450 exhibited typical difference spectrum of type I. Aniline competitively inhibited the inactivation of VX catalyzed by microsomes. These results indicate that VX is one of the substrates of mixed function oxidase. VX oxidase in the rat liver cells is exactly the mixed function oxidase.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0253-9756
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
[Aerobic metabolism of VX and mixed function oxidases].
pubmed:affiliation
Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing, China.
pubmed:publicationType
Journal Article, English Abstract