Linked Life Data

8367893

Source:http://linkedlifedata.com/resource/pubmed/id/8367893

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-10-1
pubmed:abstractText
A new cytochrome P-450 isozyme (Mr = 52,000) was purified to apparent electrophoretic homogeneity from hepatic microsomes of mice treated with acetone and its biochemical, spectral, and immunological properties characterized. Several criteria indicated that the purified cytochrome was distinct from the known mouse P-450 isozymes. The absolute spectrum of its oxidized form indicated that it was in the high spin state. In a reconstituted system, it showed low catalytic activities towards 7-ethoxycoumarin, aminopyrine, and coumarin, whereas it catalyzed the oxidation of aniline, acetone, dimethylnitrosamine with high turnover number. The mouse enzyme was immunoreactive with polyclonal antibodies against rat P-450IIE1 and exhibited an NH2-terminal aminoacid sequence with a high homology to that of rat-P-450IIE1. Based upon the above catalytic, spectral, immunological and structural properties, the purified mouse P-450 appears to be the ortholog of previously described P-450IIE1(s) of other species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0748-2337
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
539-46
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Purification and characterization of hepatic P-450IIE1 from acetone-treated mice.
pubmed:affiliation
Laboratory of Genetics and Biochemical Toxicology, CNR, Pisa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't