Findik D, Presek P
Rudolf Buchheim-Institut für Pharmakologie, Justus Liebig-Universität, Giessen, FRG.
FEBS Lett. 1988 Aug 1;235(1-2):51-6. doi: 10.1016/0014-5793(88)81232-8.
In human platelet membranes enhanced tyrosine phosphorylation of certain proteins was observed when Zn2+ instead of Mg2+ or Mn2+ was used as a divalent cation for the kinase reaction. An enhanced level of phosphate incorporation into tyrosine residues occurred into a 68 kDa polypeptide besides the 45 kDa and 105 kDa proteins. Preincubation of platelet membranes with TBR-IgG showed a concentration-dependent inhibition of the phosphorylation of the 45, 68 and 105 kDa proteins. Moreover, pp60c-src, representing the major protein tyrosine kinase activity in platelets, was found to be stimulated by Zn2+. The data, thus, support the assumption that pp60c-src kinase is responsible for Zn2+ stimulated tyrosine phosphorylation.
当在激酶反应中使用Zn2+而非Mg2+或Mn2+作为二价阳离子时，在人血小板膜中观察到某些蛋白质的酪氨酸磷酸化增强。除了45 kDa和105 kDa的蛋白质外，在一种68 kDa的多肽中，酪氨酸残基的磷酸掺入水平也有所提高。血小板膜与TBR-IgG预孵育显示，对45、68和105 kDa蛋白质的磷酸化具有浓度依赖性抑制作用。此外，代表血小板中主要蛋白质酪氨酸激酶活性的pp60c-src被发现受到Zn2+的刺激。因此，这些数据支持了pp60c-src激酶负责Zn2+刺激的酪氨酸磷酸化这一假设。
