Linked Life Data

409487

Source:http://linkedlifedata.com/resource/pubmed/id/409487

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1977-11-30
pubmed:abstractText
Trout liver microsomes contained as 0.40 nmole of cytochrome P-450 per mg of protein and a NADPH-cytochrome c reductase activity of 23 nmoles of cytochrome c reduced per mg of protein per min at 22 degrees. Associated with these was a high benzo(a)pyrene hydroxylase activity, which required NADPH and O2 and was inhibited by CO. With thin-layer chromatography, at least five metabolites could be identified (including dihydrodiols, phenols, and quinones of benzo(a)pyrene). Inhibitors such as 2-diethylaminoethyl-2,2-diphenylvalerate, aminopyrine, metyrapone, pyridine, n-octylamine, and 1,1,1-trichloro-2,2-bis(p-chlorophenyl)ethane were relatively ineffective in inhibiting trout benzo(a)pyrene hydroxylase. Typical inhibitors of 3-methylcholanthrene-induced cytochrome (P-448), such as alpha-naphthoflavone, zoxazolamine, and testosterone, were effective, however. With benzo(a)pyrene it was possible to induce type I spectral change in trout cytochrome P-450. In spite of the many enzymatic characteristics of cytochrome P-448, trout cytochrome P-450 had maximum absorbance at 450.6 nm. when in reduced form and complexed with CO. the ethyl isocyanide gave an interaction spectrum with reduced trout liver cytochrome P-450 resembling that of control rat.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3737-43
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Characterization of benzo(a)pyrene hydroxylase of trout liver.
pubmed:publicationType
Journal Article