Linked Life Data

8866616

Source:http://linkedlifedata.com/resource/pubmed/id/8866616

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1997-1-30
pubmed:abstractText
Three phospholipase A2 isoenzymes from Naja nigricollis venom inhibit the extrinsic tenase complex. We examined the role of their enzymatic activity in this inhibition by studying the effects of native and His-modified enzymes. Only CM-IV of the His-modified, catalytically inactive proteins showed significant inhibition of the activity of the complex. This indicates that strongly anticoagulant CM-IV inhibits the complex by both enzymatic and nonenzymatic mechanisms, whereas the weakly anticoagulant isoenzymes, CM-I and CM-II, inhibit primarily by catalytic degradation of phospholipids. This indicates a functional difference in the mode of inhibition between strongly and weakly anticoagulant phospholipase A2 enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1585-90
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The role of enzymatic activity in inhibition of the extrinsic tenase complex by phospholipase A2 isoenzymes from Naja nigricollis venom.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't