Linked Life Data

3827911

Source:http://linkedlifedata.com/resource/pubmed/id/3827911

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-4-1
pubmed:abstractText
A mitochondrial cytochrome P-450 fraction, which catalyzed 25-hydroxylation of vitamin D3 much more efficiently than intact mitochondria was isolated from livers of male and female rats. For comparison, a microsomal cytochrome P-450 fraction was isolated by the same procedures. The mitochondrial cytochrome P-450 from female rats catalyzed 25-hydroxylation as efficiently as the same material from male rats. The microsomal 25-hydroxylation was male specific. The 25-hydroxylase activity in intact mitochondria and the 25-hydroxyvitamin D3 concentration in serum were similar in male and female rats. There was no correlation between the 25-hydroxylase activity in microsomal cytochrome P-450 and the 25-hydroxyvitamin D3 concentration in serum.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
142
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
999-1005
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
25-hydroxylation of vitamin D3 in rat liver: roles of mitochondrial and microsomal cytochrome P-450.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't