Linked Life Data

7362832

Source:http://linkedlifedata.com/resource/pubmed/id/7362832

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-6-16
pubmed:abstractText
Platelet phosphorylase kinase (ATP:phosphorylase phosphotransferase, EC 2.7.1.38) was found to be a Ca2+-sensitive enzyme. It was two Ka values for Ca2+ viz. 0.25 and 2.6 microM, respectively. The "calcium-dependent regulator" or calmodulin can enhance the activity of phosphorylase kinase, increasing its affinity for Ca2+. In the presence of calmodulin phosphorylase kinase has only one, high affinity binding site for Ca2+ (Ka = 0.27 microM). Platelet phosphorylase kinase can be phosphorylated by endogenous cyclic AMP-dependent protein kinase increasing its catalytic activity and this activation process is reversed by dephosphorylation. The changing level of intracellular Ca2+ and cyclic AMP may control the activity of phosphorylase kinase, regulating the mobilization of glycogen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
612
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Platelet phosphorylase kinase activity and its regulation by the calcium-dependent regulatory protein, calmodulin.
pubmed:publicationType
Journal Article