Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-5-11
pubmed:abstractText
The orientation of 3-hydroxy-3-methylglutaryl coenzyme A reductase within the endoplasmic reticulum was investigated. Microsomal reductase activity was not latent, as addition of various detergents failed to activate the enzyme. Reductase activity was readily inhibited in intact microsomes by impermeable inhibitors such as trypsin, mercury dextran and anti-reductase IgG. Under the conditions used, these agents did not affect the intactness of microsomes as determined by latency of mannose-6-phosphate phosphohydrolase activity. The sensitivity to these inhibitors was not increased in disrupted microsomes. It is concluded that the domain containing the active site of the reductase is situated on the cytosolic surface of the endoplasmic reticulum.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
119
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
772-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Topography of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.