Linked Life Data

132198

Source:http://linkedlifedata.com/resource/pubmed/id/132198

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1976-9-1
pubmed:abstractText
Calcium activation of skeletal muscle sarcolemma Ca2+-ATPase is investigated. The investigation of a dependency of the initial rate of ATP hydrolysis on total concentration of substrate and on total and free calcium concentrations showed that the role of calcium ions is not limited by the formation of the substrate complex (CaATP2-). Calcium is absolutely necessary for the enzyme transition from inactive into active form. The inhibitory effect of free ATP is due to a decrease of free calcium concentration as a result of complexation with ATP, but not of competition with substrate in the active site. It is shown also that magnesium competitively inhibits the interaction of the enzyme with the substrate and non-competively suppress the activation of Ca2+-ATPase by free calcium.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
562-8
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
[Kinetic properties of skeletal muscle sarcolemmal Ca2+-ATPase].
pubmed:publicationType
Journal Article, English Abstract