Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1994-2-16
pubmed:abstractText
The Ca2+ release mechanism that triggers muscle contraction is still not completely understood. We compared Ca2+ accumulation and acetyl phosphate hydrolysis by the Ca(2+)-ATPases present in the longitudinal and junctional membrane of the sarcoplasmic reticulum of rabbit skeletal muscle and found that Ca(2+)-ATPase is more sensitive to ADP inhibition when the enzyme is located on the junctional membrane than when the enzyme is located on the longitudinal membrane (K0.5 = 144 microM for the junctional enzyme vs K0.5 = 415 microM for the longitudinal enzyme). When the enzyme was solubilized in non-ionic detergent (2% v/v Triton X-100) and tested again using 2 mM AcP as substrate, the difference in ADP sensitivity observed with native preparations disappeared. We conclude that the enzyme is regulated differently depending on its localization on the membrane of the sarcoplasmic reticulum.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0100-879X
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1113-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Difference in the sensitivity of junctional and longitudinal sarcoplasmic reticulum Ca(2+)-ATPase to ADP.
pubmed:affiliation
Departamento de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Brasil.
pubmed:publicationType
Journal Article, Comparative Study