Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-6-14
pubmed:abstractText
The tyrosine-specific protein kinase activity of pp60c-src molecules obtained from RIPA buffer lysates of human colon tumor-derived cell lines is elevated over that found in lysates from normal human colon mucosa cells. The elevation of pp60c-src kinase activity in the lysates of the cultured colon tumor cells does not appear to be the result of pp60c-src overexpression suggesting that the specific activity of the pp60c-src phosphotransferase may be enhanced. Cell-free translation of c-src mRNA from colon tumor cells and normal colon mucosa cells yielded pp60c-src molecules with similar levels of in vitro protein kinase activity suggesting that pp60c-src kinase activity in these cells may be regulated differently at a post-translational level. Analysis of pp60c-src molecules from normal colon and colon carcinoma cells revealed that they possessed indistinguishable sites and quantities of phosphorylated serine and tyrosine residues and were not detectably complexed with other cellular proteins. The activation of pp60c-src kinase activity in the colon tumor cells is associated with an apparent increase in the turnover rate of tyrosine-phosphates within the carboxyl terminal portion of the pp60c-src molecules from these tumor derived cell lines.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0890-6467
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-68
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Analysis of pp60c-src in human colon carcinoma and normal human colon mucosal cells.
pubmed:affiliation
Laboratory of Tumor Virus Biology, National Cancer Institute, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article