为了深入研究蛋白激酶Sch9的生物化学特性,在Pichiapastoris酵母KM71H茵种中分泌表达并纯化了重组Sch9蛋白.进一步通过体外磷酸化实验分析了重组Sch9蛋白的蛋白激酶活性.通过重组蛋白质工程的手段初步研究了Sch9蛋白的生物化学和酶学特性.
To facilitate the biochemical characterization of Schg, the recombinant Sch9 protein was prepared in Pichia pastoris strain KM71H. An N-terminally polyhistidine tagged protein kinase Sch9 was produced and purified via affinity chromatography. After confirming the identity of the recombinant Sch9 protein, was its enzymatic activity further analyzed by an in vitro kinase assay. Our study provides the first insight into the biochemical properties and enzymatic activity of Sch9 via a recombinant protein engineering approach.