Komov V P, Strelkova M A
Biokhimiia. 1987 Jul;52(7):1080-6.
The Mg,ATP-dependent serine proteinase (Mr = 50 kD; pH optimum 8.0) was isolated and purified 750-fold. The substrate specificity of the enzyme to some protein substrates (catalase, aldolase, uratoxidase, superoxide dismutase, albumin, cytochrome c, insulin) was investigated. The proteinase shows an affinity for proteins whose molecular mass is more than 100 kD. Some quantitative parameters of the enzyme metabolism, e.g., rate constants for synthesis and degradation of serine proteinase and the time of functioning of the de novo synthesized protein, were investigated.
分离并纯化了镁离子、ATP 依赖性丝氨酸蛋白酶（分子量 50 kD；最适 pH 8.0），纯化倍数达 750 倍。研究了该酶对一些蛋白质底物（过氧化氢酶、醛缩酶、尿酸氧化酶、超氧化物歧化酶、白蛋白、细胞色素 c、胰岛素）的底物特异性。该蛋白酶对分子量超过 100 kD 的蛋白质具有亲和力。研究了该酶代谢的一些定量参数，例如丝氨酸蛋白酶合成和降解的速率常数以及新合成蛋白质的作用时间。
