Linked Life Data

7107600

Source:http://linkedlifedata.com/resource/pubmed/id/7107600

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1982-10-21
pubmed:abstractText
Interaction of purified bovine milk lipoprotein lipase (LpL) with sonicated vesicles of dipalmitoyl phosphatidylcholine in the gel phase is associated with an increase in the rate of the LpL-catalyzed hydrolysis of p-nitrophenyl butyrate. There is a 6-fold increase in Vmax. Apolipoprotein C-II, the activator protein for LpL, inhibits the LpL-catalyzed hydrolysis of p-nitrophenyl butyrate. With 0.5 mol % tri[14C]oleoylglycerol present in the dipalmitoyl phosphatidylcholine vesicles and in the presence of 20 mM Ca2+, the rate of p-nitrophenyl butyrate hydrolysis is decreased reciprocally compared to trioleoylglycerol hydrolysis and is dependent on apolipoprotein C-II. These results suggest that apolipoprotein C-II enhances the activity of LpL by increasing the affinity of the active site of LpL for triacylglycerol.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10200-3
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Reciprocal effect of apolipoprotein C-II on the lipoprotein lipase-catalyzed hydrolysis of p-nitrophenyl butyrate and trioleoylglycerol.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.