|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
1979-2-12
|
|
pubmed:abstractText |
A regulation mechanism of the interaction of microsomal oxidases and mitochondrial respiratory chain with oxidase substrates is suggested. Quantitative comparison of their affinity to microsomal oxidases and mitochondrial NADH-dehydrogenase is carried out. The interaction with both systems is found to be hydrophobic. It is found that microsomal oxidase substrates inhibit mitochondrial NADH-dehydrogenase at concentrations, which should completely fill the active site of cytochrome P-450. It is suggested that redistribution of reduced equivalents from mitochondria to microsomes and the acceleration of xenobiotic detoxication take place.
|
|
pubmed:language |
rus
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0320-9725
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
43
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1809-15
|
|
pubmed:dateRevised |
2007-7-23
|
|
pubmed:meshHeading |
pubmed-meshheading:214167-Barbiturates,
pubmed-meshheading:214167-Cytochrome P-450 Enzyme System,
pubmed-meshheading:214167-Electron Transport,
pubmed-meshheading:214167-Endoplasmic Reticulum,
pubmed-meshheading:214167-Lipids,
pubmed-meshheading:214167-Microsomes,
pubmed-meshheading:214167-Mitochondria,
pubmed-meshheading:214167-NAD,
pubmed-meshheading:214167-NADH, NADPH Oxidoreductases,
pubmed-meshheading:214167-Oxidoreductases,
pubmed-meshheading:214167-Solubility
|
|
pubmed:year |
1978
|
|
pubmed:articleTitle |
[Regulatory interaction between the respiratory chain of mitochondria and the oxidative system of the endoplasmic reticulum].
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
English Abstract
|
