Linked Life Data

7068649

Source:http://linkedlifedata.com/resource/pubmed/id/7068649

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1982-6-24
pubmed:abstractText
Two protein kinases (MPK1 and MPK2) were isolated from bovine heart mitochondria. After the solubilization of submitochondrial particles with cholate, these protein kinases were purified by ammonium sulfate precipitation, Sepharose 6B gel filtration, and affinity chromatography on phosvitin-Sepharose. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the final preparation of MPK1 contained two major polypeptide bands (40,000 and 36,000 daltons). MPK2 contained one major polypeptide of 34,000 daltons. Under nondenaturing conditions, the molecular weights of MPK1 and MPK2 were estimated to be approximately 250,000 and 70,000-90,000, respectively. MPK1 had a pH optimum at 9.0 and MPK2 at 7.5. Both enzymes required Mg2+ for activity and responded poorly to Mn2+ or Ca2+. Both had similar apparent Km values for ATP and were not affected by either cyclic AMP or Ca2+-calmodulin. MKP1 phosphorylated threonine residues and MPK2 serine residues of casein. With beta casein as substrate, MPK1 was more active than MPK2, whereas with alpha casein, MPK2 was more active than MPK1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4547-51
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification and characterization of two protein kinases from bovine heart mitochondrial membrane.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.