Linked Life Data

1479780

Source:http://linkedlifedata.com/resource/pubmed/id/1479780

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-2-8
pubmed:abstractText
By means of NED-affinity column chromatography, two distinct protein kinases have been selectively purified from the crude membrane extract of mouse brain. One (designated P-I kinase) was eluted from the column by the buffer containing 5 mM EGTA and the other (designated P-II kinase) was eluted by the buffer containing 0.6 M KCl. The activity of A-kinase was detected in the column passed through fraction. Biochemical characteristics of P-I and P-II kinases corresponded exactly to those of C-kinase and casein kinase II (CK-II), respectively. In addition, immunoprecipitate experiment using anti-CK-II antiserum against the beta-subunit of Drosophila CK-II showed that P-II kinase is identical to CK-II and the 62 kDa cellular polypeptide is associated with the kinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0023-1924
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-11
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Selective purification of two distinct protein kinases (C-kinase and casein kinase II) from the membrane fraction of mouse brain by NED-affinity column chromatography.
pubmed:affiliation
Department of Pharmacological Sciences, Tohoku University Hospital, Sendai, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't