Linked Life Data

6687681

Source:http://linkedlifedata.com/resource/pubmed/id/6687681

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-5-5
pubmed:abstractText
The Ca2+- and calmodulin-dependent myosin light chain kinase of rabbit skeletal muscle was converted to a Ca2+-independent form by limited proteolysis with alpha-chymotrypsin. The conditions prevailing during proteolysis are important and the loss of Ca2+-dependence was achieved best by hydrolysis of the Ca2+-calmodulin-kinase complex. The lack of Ca2+- and calmodulin-dependence was found using both myosin and isolated light chains as substrates. The specific activity of the Ca2+-independent form (Mr approximately 65,000) was similar to that of the native enzyme, i.e., 2 to 5 mumol phosphate transferred min-1 mg-1 kinase. The 65,000-dalton fragment was phosphorylated by the catalytic subunit of the cAMP-dependent protein kinase and approximately 0.8 moles phosphate were incorporated per fragment.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
701-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Conversion of a Ca2+-dependent myosin light chain kinase from skeletal muscle to a Ca2+-independent form.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.