Linked Life Data

6548160

Source:http://linkedlifedata.com/resource/pubmed/id/6548160

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-11-1
pubmed:abstractText
The dithioester analog of dihexanoylphosphatidylcholine, rac-1,2-S,S-dihexanoyl-3-phosphocholine-1,2-dimercapto-3-propanol was synthesized and compared to the corresponding acyl-oxyester lipid as a substrate for bovine milk lipoprotein lipase. The apparent maximal reaction velocity (Vmax) for dihexanoyldithiophosphatidylcholine was considerably lower than that for dihexanoylphosphatidylcholine (0.12 vs. 5.0 mumol product released/min per mg lipoprotein lipase, respectively). The apparent Km values were 1.9 and 4.0 mM, respectively. 3-Butyrylthio-1,2-dibutyryloxypropane was also compared to tributyrylglycerol as a substrate for lipoprotein lipase; hydrolysis of the acyl-thioester bond was insignificant when compared to the corresponding oxyester derivative. Apolipoprotein C-II, the activator protein of lipoprotein lipase for long-chain fatty acyl substrates, had no effect on the hydrolysis of either the thio- or oxyester short-chain substrates. The low lipoprotein lipase activity for the thioester substrates is discussed in relation to the structure of the lipid and the active site of the enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
795
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-20
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Comparison of acyl-oxyester and acyl-thioester lipids as substrates for bovine milk lipoprotein lipase.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.