Linked Life Data

15618659

Source:http://linkedlifedata.com/resource/pubmed/id/15618659

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-12-27
pubmed:abstractText
A cDNA clone designated as CYP2C43 was isolated from the rhesus monkey liver cDNA library. The first 16 amino acid residues at the N-terminal region of this cDNA product were identical with those of P450 CMLd which have been purified and characterized as S-mephenytoin 4'-hydroxylase in monkey liver. The respective nucleotide and deduced amino acid sequences of CYP2C43 were 83% and 77%, identical to those of monkey CYP2C20. Antibody against CYP2C9 detected a protein in the microsomes of yeast transformed CYP2C43 expression plasmid. The specific content of recombinant CYP2C43 was 78.0 pmol/mg protein and the yield was 4.23 nmol/l of the culture. CYP2C43 was able to metabolize S-mephenytoin stereo-selectively. The activity for S-mephenytoin in the microsomes reconstituted with or without cytochrome b(5) was found to be 96.2 or 23.7 pmol/min/nmol P450, respectively. CYP2C43, however, did not show any oxidative activity for tolbutamide. These results indicate that CYP2C43 is the second identified member of the monkey CYP2C subfamily and a cDNA clone encoding P450 CMLd in monkey.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:issn
1347-4367
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
117-24
pubmed:year
2002
pubmed:articleTitle
Molecular cloning of monkey CYP2C43 cDNA and expression in yeast.
pubmed:affiliation
Division of Pharmacy, Shinshu University Hospital, Matsumoto, Japan.
pubmed:publicationType
Journal Article