Linked Life Data

2235974

Source:http://linkedlifedata.com/resource/pubmed/id/2235974

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-12-7
pubmed:abstractText
The primary structure of the carboxy terminal 296 amino acids of chicken cholesterol side chain cleavage cytochrome P450 (P450scc) was deduced from a partial cDNA clone isolated from a chicken ovarian cDNA library. The sequence contained putative steroid binding and heme binding regions. Comparison of this sequence with the corresponding sequences of three mammalian forms of P450scc shows greater than 50% homology. The heme binding region of the avian P450scc shows 76% homology with the heme binding regions of rat and human P450scc and 81% homology with that of bovine P450scc.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0931-9506
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Deduced amino acid sequence of heme binding region of chicken cholesterol side chain cleavage cytochrome P450.
pubmed:affiliation
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't