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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1997-2-27
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pubmed:abstractText |
Calmodulin-dependent protein kinase II was purified to apparent homogeneity with a high yield from the total calmodulin-binding protein fraction of bovine cardiac muscle in a single step by gel filtration column chromatography. This procedure is simple and suitable for adaptation to large scale preparations. The purified calmodulin-dependent protein kinase has a specific enzymic activity of 2.4 mumol/min/mg when mixed histone was used as a substrate. The preparation of enzyme appears to be homogeneous when examined by SDS-PAGE. The molecular weight of the enzyme was determined to be 570 kDa by gel filtration. SDS-PAGE of the enzyme subunit showed a single protein band with an apparent molecular weight of 56 kDa. These results suggest that the calmodulin-dependent protein kinase II from bovine heart is composed of 10 identical subunits. Anti-peptide antibody raised against multifunctional calmodulin-dependent protein kinase II from rat brain showed a single immunoreactive band of 56 kDa on Western blot. These results suggested that bovine cardiac muscle calmodulin-dependent protein kinase could resemble the brain isozyme. Calmodulin-dependent protein kinase II undergoes autophosphorylation with a maximal incorporation of 1 mol of phosphate per mol of the subunit of the enzyme and the autophosphorylated enzyme remains active in the absence of Ca2+ and calmodulin. The concentration of Ca2+ required for the activation of calmodulin-dependent protein kinase II depends on the level of calmodulin in the reaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acrylic Resins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Sephacryl Superfine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0143-4160
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
347-53
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8939354-Acrylic Resins,
pubmed-meshheading:8939354-Amino Acid Sequence,
pubmed-meshheading:8939354-Animals,
pubmed-meshheading:8939354-Antibody Specificity,
pubmed-meshheading:8939354-Blotting, Western,
pubmed-meshheading:8939354-Calcium,
pubmed-meshheading:8939354-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:8939354-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:8939354-Caseins,
pubmed-meshheading:8939354-Cattle,
pubmed-meshheading:8939354-Chromatography,
pubmed-meshheading:8939354-Enzyme Activation,
pubmed-meshheading:8939354-Isoenzymes,
pubmed-meshheading:8939354-Molecular Sequence Data,
pubmed-meshheading:8939354-Molecular Weight,
pubmed-meshheading:8939354-Myocardium,
pubmed-meshheading:8939354-Phosphorylation
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pubmed:year |
1996
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pubmed:articleTitle |
Calmodulin-dependent protein kinase II from bovine cardiac muscle: purification and differential activation by calcium.
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pubmed:affiliation |
Department of Pathology, Saskatoon Cancer Centre, College of Medicine, University of Saskatchewan, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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