Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1997-10-14
pubmed:abstractText
Two different protein tyrosine kinases were detected in the cytosolic fraction of different human tumor tissues. After partial purification, the two enzymes, which were highly active in breast tumor tissues, were characterized. One of them, soluble tyrosine kinase-1 (STK-1), represents a soluble form of the c-Src protein, which is apparently underphosphorylated on its C-terminal tyrosine residue whereas the other (STK-2) is a 48-kDa protein tyrosine kinase (PTK), which is molecularly and functionally related to the C-terminal Src kinase (Csk). These two protein tyrosine kinases clearly exhibit a different substrate specificity, and are responsible for the high tyrosine kinase activity present in the cytosolic fraction of human breast cancer. In addition, it was observed that STK-1 and STK-2 are also expressed in the breast cancer cell line, CAL-51.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0143-3334
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1463-72
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Characterization of two different cytoplasmic protein tyrosine kinases from human breast cancer.
pubmed:affiliation
Laboratoire de Biochimie des Régulations Cellulaires Endocrines, INSERM Unite 244, DBMS, CEA, Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't