非受体酪氨酸激酶ARG与过氧化氢酶相互作用机制的初步研究

Interaction of non-receptor tyrosine kinase Arg and catalase

通过体外结合实验,发现Arg蛋白与过氧化氢酶之间有相互作用,且这种作用是通过Arg蛋白的SH3结构域和过氧化氢酶的P290FNP介导的。利用体外激酶分析和Western印迹证明Arg蛋白可以使过氧化氢酶磷酸化。本研究为过氧化氢酶的活性调控研究奠定了基础。

Interaction of non-receptor tyrosine kinase Arg with catalase was demonstrated by in vitro fishing experiments.The interaction was mediated by binding of Arg SH3domain with P290FNP site in catalase.Catalase could be phosphory-lated by Arg as demonstrated by in vitro kinase assay and immunoblotting with anti-phosphorylated tyrosine.