Linked Life Data

6130787

Source:http://linkedlifedata.com/resource/pubmed/id/6130787

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-4-7
pubmed:abstractText
Quenching of the fluorescence of the (Ca2+ + Mg2+)-ATPase purified from muscle sarcoplasmic reticulum can be used to measure relative binding constants of hydrophobic compounds to the phospholipid-protein interface. We show that the binding constant for cholesterol is considerably less than that for phosphatidylcholine, so that cholesterol is effectively excluded from the phospholipid annulus around the ATPase. However, dibromocholestan-3 beta-ol causes quenching of the fluorescence of the ATPase, and so has access to other, non-annular sites. We suggest that these non-annular sites could be at protein/protein interfaces in ATPase oligomers. Oleic acid can bind at the phospholipid/protein interface, although its binding constant is less than that for a phosphatidylcholine, and it can also bind at the postulated non-annular sites. The effects of these compounds on the activity of the ATPase depend on the structure of the phospholipid present in the systems.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
693
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
398-406
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Annular and non-annular binding sites on the (Ca2+ + Mg2+)-ATPase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't