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18.97.14.90
18.97.14.90
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SCIE SCOPUS
Biochemical and Genetic Studies on Tyrosine Kinases in Normal and Malignant Tissue : Identification and Functional Characterization of New Tyrosine Kinases
( H . Rubsamen Waigmann )
UCI I410-ECN-0102-2009-470-007038822
This article is 4 pages or less.

In 1987, we had identified a new gene from a cDNA-library derived from chicken spleen, which had a mRNA identical in size to the mRNA of c-src, but was genetically clearly distinct. The new gene was most closely related to Ick and hence was named tkl (tyrosine-kinase related to Ick). Due to a mRNA of the same size and the cross-hybridization with the kinase domain of c-src, some of the earlier work on c-src expression actually appears to have detected c-tkl: With probes specific for the N-termini of the genes, we were not able to detect src message in spleen, but only tkl. Like other genes of the proteinkinase family, c-tkl is evolutionarily conserved. Bands were found in Southern blots down to carp and shark, but not in the DNA of tunicates or lamprey. Expression of the protein in a baculo virus system allowed to biochemically demonstrate that it is a tyrosine kinase which auto-phosphorylates on tyrosine. The protein is fairly acidic, with a pl around 5. As in vitro substrate it did not accept enolase nor caseine, and in this respect differed from src. Apart from tkl, two tyrosine kinase genes were identified in human lung by using degenerate primers within the conserved kinase region of protein tyrosine kinases for PCR. One of these new protein kinase genes belongs to the receptor family of tyrosine kinases which is defined by PDGF.

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