Linked Life Data

8335109

Source:http://linkedlifedata.com/resource/pubmed/id/8335109

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-8-24
pubmed:abstractText
Glycosyl-phosphatidylinositol-specific phospholipase D (GPI-PLD) is an amphiphilic protein which, in serum, is associated with high-density lipoproteins (HDL). It is shown that the major component of the HDL fraction, apolipoprotein A-I (apo A-I), is responsible for this association. In the absence of apo A-I, purified GPI-PLD occurred as virtually inactive aggregates which became disaggregated by apo A-I. The enzyme/apo A-I complex efficiently hydrolyzed the solubilized GPI-anchored substrate, acetylcholinesterase. Triton X-100 was also able to dissociate aggregated GPI-PLD, however, it strongly inhibited enzyme activity at detergent concentrations above the critical micellar concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
327
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
203-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Glycosyl-phosphatidylinositol-specific phospholipase D. Interaction with and stimulation by apolipoprotein A-I.
pubmed:affiliation
Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't