Linked Life Data

6391493

Source:http://linkedlifedata.com/resource/pubmed/id/6391493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1985-1-17
pubmed:abstractText
Rat liver cytosol was shown previously by us to contain multiple forms of 3 alpha-hydroxysteroid dehydrogenase. Two (F4-II and -III) of the seven forms were purified to homogeneity, and four (F3-II, -III, -IV and F4-I) of them partially purified. One of them (F4-III) has been shown previously to catalyze the reduction of long-chain aliphatic and aromatic aldehydes or aromatic ketones as well as 3-oxosteroids [M. Ikeda et al., Biochem. Pharmac. 30, 1931 (1981)]. The reducing activity of such compounds was examined with the other F4 enzymes, and it was revealed that they also reduce a number of carbonyl compounds described above. In addition, quinones were tested for the first time in this report as substrates for all the F4 enzymes, and among them 9,10-phenanthrenequinone was found to be the best substrate for them, followed by hydrindantin and 2,6-dichlorophenolindophenol, while menadione was a poor substrate. The F4 enzymes did not catalyze the reduction of the oxo group at the 9-position of the prostaglandins of the E and A class with NADPH or NADH. On the basis of this evidence, the identity of ketone reductases (F4-I-III) in the rat liver is proposed to be 3 alpha-hydroxysteroid dehydrogenase, rather than prostaglandin 9-ketoreductase, which was demonstrated to correspond to ketone reductase in human brain [B. Wermuth, J. biol. Chem. 256, 1206 (1981)].
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3957-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Properties of NADPH-dependent carbonyl reductases in rat liver cytosol.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't