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  • Title: Identification of a novel protein tyrosine kinase that phosphorylates pp60c-src and regulates its activity in neonatal rat brain.
    Author: Okada M, Nakagawa H.
    Journal: Biochem Biophys Res Commun; 1988 Jul 29; 154(2):796-802. PubMed ID: 2456763.
    Abstract:
    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.
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