Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-12-18
pubmed:abstractText
We examined the effects of P1,P5-di(adenosine-5')pentaphosphate (Ap5A), a potent inhibitor of adenylate kinase, on fragmented sarcoplasmic reticulum (FSR) obtained from bullfrog skeletal muscle in view of the possible usefulness of the nucleotide in experiments with FSR to avoid complications due to contaminating adenylate kinase. Ap5A itself does not cause Ca uptake in the place of ATP. It inhibited adenylate kinase activity without affecting the Ca-ATPase or Ca uptake activity of FSR. The observed effect was a competitive inhibition of basic ATPase activity of the light fraction of FSR. Therefore, P1,P5-di(adenosine-5')pentaphosphate represents an extremely useful tool in experiments wth fragmented sarcoplasmic reticulum, such as studies of H+ movement accompanying Ca movement, ATP-ADP exchange reaction, and calorimetry of the Ca uptake process. A rather high concentration (50 muM or more) of Ap5A is required for complete inhibition of adenylate kinase. Further, we detected 1.3-2.8 nmol of (ATP + ADP), 2-4 nmol of Pi, and unidentified metal(s) in 50 nmol of Ap5A, and Ap5A is more labile to acid and molybdate than ATP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
871-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
P1,P5-Di(adenosine-5')pentaphosphate(Ap5A) as an inhibitor of adenylate kinase in studies of fragmented sarcoplasmic reticulum from bullfrog skeletal muscle.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't