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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1976-9-25
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pubmed:abstractText |
Lipoprotein lipase from dialyzed and lyophilized bovine skim milk hydrolyses specifically the ester in position 1 of triacylglycerols and of enantiomeric alkyldiacylglycerols. No such specificity could be observed when enantiomeric dialkylacylglycerols were used as substrates since hydrolysis in positions 1 and 3 occurred at the same rate. Dialkylacylglycerols are, therefore, unsuitable as model substrates for the assay of the stereospecificity of lipases.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
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pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
431
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
359-62
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:945746-Animals,
pubmed-meshheading:945746-Cattle,
pubmed-meshheading:945746-Kinetics,
pubmed-meshheading:945746-Lipoprotein Lipase,
pubmed-meshheading:945746-Milk,
pubmed-meshheading:945746-Stereoisomerism,
pubmed-meshheading:945746-Structure-Activity Relationship,
pubmed-meshheading:945746-Triglycerides
|
pubmed:year |
1976
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pubmed:articleTitle |
Stereospecificity of lipases. Enzymatic hydrolysis of enantiomeric alkyldiacyl- and dialkylacylglycerols by lipoprotein lipase.
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pubmed:publicationType |
Journal Article
|