Linked Life Data

687655

Source:http://linkedlifedata.com/resource/pubmed/id/687655

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1978-11-27
pubmed:abstractText
In intestinal epithelial cells, three enzymes possessing monoacylglycerol hydrolase activity were found and partially purified. Two of these enzymes have properties that justify their classification as an esterase and one as a monoacylglycerol lipase. The three enzymes show similar Km values for monooleoylglycerol and each shows similar activity towards 1- and 2-monopalmitoylglycerol. Antiserum raised in rabbits against rat liver monoacylglycerol lipase inhibits the intestinal lipase completely, suggesting that the enzymes are at least partially similar. The esterases of small intestinal villus cells were not inhibited by the antiserum against liver monoacylglycerol lipase. It was calculated that the esterases account for approx. 2/3 of the monooleoylglycerol hydrolase activity in epithelial cells. Monoacylglycerol lipase also hydrolyzed palmitoyl-CoA, while the esterases did not. The enzymes were inhibited by micellar palmitoyl-CoA. The hypothesis that palmitoyl-CoA is an important regulator for monoacylglycerol acylation is discussed in the light of these new findings.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
530
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
56-66
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Partial purification and properties of monoacylglycerol lipase and two esterases from isolated rat small intestinal epithelial cells.
pubmed:publicationType
Journal Article