Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1977-9-22
pubmed:abstractText
A soluble rat liver protein, termed "supernatant protein factor" (SPF), that stimulates microsomal squalene epoxidase has been purified approximately 11,000-fold. The most highly purified preparation obtained by isoelectric focusing shows a single coincident peak for activity and protein (the isoelectric point, pI, was 6.74). SPF is about 95% pure, judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and it migrates to a position corresponding to an apparent molecular weight of 47,000. An amino acid analysis of SPF is presented, and the properties of SPF and of the various soluble protein activators of microsomal sterol biosynthesis described by other laboratories are compared.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5381-5
pubmed:dateRevised
2009-10-27
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Purification and properties of a soluble protein activator of rat liver squalene epoxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.