Linked Life Data

7236650

Source:http://linkedlifedata.com/resource/pubmed/id/7236650

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-8-10
pubmed:abstractText
The rates of reaction of human lipoprotein lipase (EC 3.1.1.34) with triacylglycerol and partial acylglycerol substrates have been compared as a function of the concentration of lipase cofactor protein (apolipoprotein C-II). The data indicate that the dissociation constant for monoacylglycerol is approximately three orders of magnitude greater than for diacylglycerols, indicating that only when the concentrations of higher acylglycerols become vanishingly small will significant monoacylglycerol hydrolysis (from 1-monoacylglycerol generated by isomerization of the 2-substituted primary product) be mediated by the lipase. This is in spite of the fact that maximal reaction velocities with each of the potential substrates are similar. A 'lipolytic cycle' is proposed to explain binding and dissociation of substrates with cofactor-lipase complex during catabolism of triacylglycerols.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
620
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
440-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Characteristics of triacylglycerol and partial acylglycerol hydrolysis by human plasma lipoprotein lipase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.