Linked Life Data

7074125

Source:http://linkedlifedata.com/resource/pubmed/id/7074125

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-7-8
pubmed:abstractText
Highly purified rat hepatic lipase (NaCl-resistant, alkaline pH optimum) was studied to evaluate whether the enzyme has triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities. Enzyme exhibiting a single band by SDS-polyacrylamide gel electrophoresis and having a specific activity eight times greater than that in any previous report was utilized. The ratios of the different lipolytic activities to each other remained constant throughout a multistep hepatic lipase purification. The lipolytic activities coeluted by gel filtration on Ultrogel AcA 34. Column isoelectric focusing of the highly purified enzyme revealed comigration of the lipolytic activities. Thermal inactivation produced similar decay curves for the different activities. Immune titration curves for the different activities with specific antibody against hepatic lipase were essentially identical. These findings indicate that hepatic lipase is a single enzyme molecule which has triacyglycerol lipase, monoacylglycerol lipase and phospholipase activities with artificial substrates. To study these lipolytic activities further, purified hepatic lipase was subjected to limited digestion by specific proteases. The triacylglycerol lipase activity was more sensitive to proteolytic destruction than either of the other two activities.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
710
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
464-70
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities of highly purified rat hepatic lipase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.