Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-6-24
pubmed:abstractText
1. Components of the hepatic monooxygenase systems (cytochrome P-450, cytochrome b5, NADPH cytochrome P-450- or c-reductase) of the brown trout (Salmo trutta), leopard frog (Rana pipiens) and garter snake (Thamnophis) were considerably lower than those found in the rat. 2. Reactivity of snake NADPH-cytochrome P-450-reductase with cytochrome P-450 was about twice that of the rat reductase; reactivities of trout and frog reductases were similar, but lower than that of the rat. The optimal temperature for the rat, frog and snake reductase activity was 37 degrees C, but 26 C for the trout reductase, regardless of whether cytochrome P-450 or cytochrome c was the electron acceptor for the reaction. 3. A type I substrate (benzphetamine) and a type II substrate (aniline) were less reactive with P-450 cytochrome from the trout, frog and snake than with P-450 cytochrome from the rat. 4. Qualitative differences were seen in the ethylisocyanide spectrum of microsomes from the rat, trout, frog and snake; these differences reflect qualitative differences in the populations of P-450 cytochromes among each of the four species.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Hepatic cytochrome P-450-dependent monooxygenase systems of the trout, frog and snake--I. Components.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.