Linked Life Data

6685296

Source:http://linkedlifedata.com/resource/pubmed/id/6685296

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1983-12-20
pubmed:abstractText
Liver microsomes from rabbits treated chronically with ethanol were solubilized and fractionated to yield a new isozyme of cytochrome P-450 in a homogeneous state. This cytochrome, designated as isozyme 3a on the basis of its relative electrophoretic mobility, is distinct from the known terminal amino acid sequences. In addition, peptide mapping by high performance liquid chromatography following trypsinolysis indicates that form 3a is a unique gene product. This cytochrome has unusually high activity in the oxidation of ethanol and other alcohols to aldehydes and in the rho-hydroxylation of aniline as compared with the other isozymes of P-450. The ethanol-oxidizing activity of isozyme 3a, which requires the presence of NADPH and NADPH-cytochrome P-450 reductase and is stimulated by the presence of phosphatidylcholine, is not due to contamination by catalase or an NAD+-or NADP+-dependent alcohol dehydrogenase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0091-3057
pubmed:author
pubmed:issnType
Print
pubmed:volume
18 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Alcohol oxidation by isozyme 3a of liver microsomal cytochrome P-450.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.