Linked Life Data

2456763

Source:http://linkedlifedata.com/resource/pubmed/id/2456763

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-9-2
pubmed:abstractText
A novel protein tyrosine kinase not related to pp60c-src, designated as N-PTK, has recently been found in neonatal rat brain. In the present study, the enzyme was purified further by heparin-Sepharose column chromatography, and identified as a monomer protein with a Mr of 47 K and a pI of 7.0 by two-dimensional gel electrophoresis. The enzyme was found to phosphorylate purified pp60c-src at a tyrosine residue(s). The major phosphorylation site was shown by alpha-chymotryptic peptide mapping to be in the carboxy terminal V8 protease fragment (V2), but to be different from the autophosphorylation site, Tyr-416. The phosphorylation significantly suppressed pp60c-src activity with enolase as a substrate. These findings strongly suggest that N-PTK is a specific kinase that phosphorylates pp60c-src and regulates its function in the cell.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
796-802
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Identification of a novel protein tyrosine kinase that phosphorylates pp60c-src and regulates its activity in neonatal rat brain.
pubmed:affiliation
Division of Protein Metabolism, Osaka University, Suita, Japan.
pubmed:publicationType
Journal Article