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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1986-3-19
|
pubmed:abstractText |
The secretion of lipoprotein lipase has been examined in Ob17 adipose cells. No spontaneous secretion is detected. The activity of the heparin-releasable enzyme shows a first-order process of inactivation. This constant rate of inactivation, coupled with a decreased rate of secretion, prevents any significant determination of enzyme secretion in heparin-containing media. Thus, a perifusion system, with which the rate of enzyme inactivation is minimal and systematic, has been devised and used. The data show that the secretion of a pool of pre-existing lipoprotein lipase molecules is followed by the secretion of newly synthesized enzyme molecules. The results are discussed with respect to the significance of the determinations of the heparin-releasable enzyme in most studies as well as with respect to the intracellular localization of lipoprotein lipase in Ob17 cells.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
12
|
pubmed:volume |
875
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
324-33
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading | |
pubmed:year |
1986
|
pubmed:articleTitle |
A continuous flow method for the study of lipoprotein lipase secretion in adipose cells.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|