Linked Life Data

2590203

Source:http://linkedlifedata.com/resource/pubmed/id/2590203

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-12-28
pubmed:abstractText
A cDNA clone encoding for the bovine pancreatic cholesterol esterase has been sequenced. Pancreatic cholesterol esterases hydrolyze dietary cholesterol esters to cholesterol and free fatty acids, which are then absorbed from the gut. Northern blots reveal that the positive signal at 1.9 kilobases is much more intense in the cow than in calf pancreas, indicating that the induction of the enzyme is due to increased transcription or stability of mRNA. The primary structure of this enzyme is similar to that of the rat pancreatic lysophospholipase. We found that homogeneous human and bovine pancreatic cholesterol esterases have high levels of lysophospholipase activity, indicating that these two activities reside within the same protein. Therefore, the metabolism of dietary neutral lipids and polar lipids may be linked through a single enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
164
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1302-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase.
pubmed:affiliation
Department of Medicine, Jewish Hospital of St. Louis, Washington University Medical Center, Missouri 63110.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.