Linked Life Data

3654625

Source:http://linkedlifedata.com/resource/pubmed/id/3654625

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1987-11-9
pubmed:abstractText
Previous work from this laboratory and others has shown that the hydrolysis of pure dipalmitoylphosphatidylcholine (DPPC) liposomes by porcine pancreatic phospholipase A2 in the vicinity of the gel-to-liquid crystal phase transition is characterized by a slow initial phase followed by an apparent burst of activity. In this article we report a detailed quantitative analysis of the early time course of the hydrolysis of dipalmitoylphosphatidylcholine large unilamellar vesicles at 38 degrees C. Several kinetic models to quantitatively describe the data were considered. The most conservative model consistent with the kinetic data is one in which the enzyme initially binds the bilayer and becomes activated via a process that requires the formation of protein dimers on the surface of the membrane. The relevant kinetic parameters of the model are reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13476-82
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The activation of porcine pancreatic phospholipase A2 by dipalmitoylphosphatidylcholine large unilamellar vesicles. Analysis of the state of aggregation of the activated enzyme.
pubmed:affiliation
Department of Biochemistry, University of Virginia School of Medicine, Charlottesville 22908.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.