Linked Life Data

8123254

Source:http://linkedlifedata.com/resource/pubmed/id/8123254

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7-8
pubmed:dateCreated
1994-4-14
pubmed:abstractText
The calcium-dependent ATPase from sarcoplasmic reticulum of rabbit has been purified and reconstituted in dispersions containing pure phosphatidylcholines. Each phosphatidylcholine (PC) had palmitate (16:0) at the sn-1 position of glycerol and stearate (18:0), oleate (18:1), linoleate (18:2), arachidonate (20:4), or docosahexaenoate (22:6) at the sn-2 position. The activities and activation energies of the enzyme indicated that the best enzyme function occurred when 16:0-18:1 PC or 16:0-18:2 PC was the lipid in which the ATPase was embedded. Circular dichroism measurements made as a function of temperature suggested that the protein in 16:0-18:0 and 16:0-18:1 PC behaved most like sarcoplasmic reticulum or purified ATPase. The results suggest that there may be an optimal lipid environment for the ATPase which is provided by 16:0-18:1 PC and 16:0-18:2 PC, the two most common lipids of the sarcoplasmic reticulum.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0829-8211
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
381-9
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
Reconstitution of rabbit sarcoplasmic reticulum calcium ATPase in a series of phosphatidylcholines containing a saturated and an unsaturated chain: suggestion of an optimal lipid environment.
pubmed:affiliation
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't