Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-2-22
pubmed:abstractText
An intracellular form of phospholipase A2 was purified about 47,500-fold to near homogeneity from bovine platelets 100,000 x g supernatant by sequential use of column chromatographies on Heparin-Sepharose, DEAE-Sephacel, Butyl-Toyopearl, Sephacryl S-300, DEAE-5PW HPLC, TSK G 3000 SW HPLC and Mono Q FPLC. The final preparation showed a single band on SDS-polyacrylamide gel, and its molecular mass was estimated to be approximately 100,000 daltons. The purified PLA2 showed maximal activity at alkaline pH(pH 9.0-10.0) and considerable activity at 0.3-1.0 microM calcium concentration. It hydrolyzed phosphatidylcholine containing arachidonate at sn-2 position with high selectivity in comparison to linoleate.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
189-96
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Purification and some properties of a phospholipase A2 from bovine platelets.
pubmed:affiliation
Department of Life Science, Pohang Institute of Science and Technology, Hyoja-dong, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't