Linked Life Data

3377769

Source:http://linkedlifedata.com/resource/pubmed/id/3377769

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-6-24
pubmed:abstractText
Biochemical properties of a cytosolic protein-tyrosine kinase (CPTK-40) partially purified from porcine spleen were characterized and compared with p40 kinase, a cytosolic protein-tyrosine kinase from bovine thymus. When CPTK-40 was incubated with MnCl2 and (gamma-32P)ATP, only a phosphoprotein with a molecular weight of 40 kilodalton was observed. CPTK-40 efficiently phosphorylated tubulin with the rate of 0.5 nmol/min/mg. Unlike p40 kinase, casein was also a substrate for CPTK-40. Among various divalent cations tested, Co2+, Mn2+ and Mg2+ were effective metal ions for the enzyme activity. Ca2+ could also serve as a divalent cation for the activity although the rate was low. These results suggest that CPTK-40 is similar but not identical to p40 kinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
152
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1123-30
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Characterization of partially purified cytosolic protein-tyrosine kinase from porcine spleen.
pubmed:affiliation
Department of Biochemistry, Fukui Medical School, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't