Kolodzeĭskaia M V
Ukr Biokhim Zh (1978). 1986 Mar-Apr;58(2):90-104.
Recent data on the effect of serine proteinases of lower vertebrates are generalized. Hydrolysis specificity and kinetics of different synthetic substrates, dependence of the activity of enzymes on pH, their irreversible inhibition by chloromethyl ketones of amino acids and peptides as well as high-molecular proteinase inhibitors are considered in detail. The data testify to the fact that chymotrypsins and trypsins of higher vertebrates and serine proteinases of lower vertebrates act as an acid-base catalysis. Enzymes in the pyloric cacca of fishes are in the state of proenzymes and are transformed into an active form with the aid of their own proteolytic factors. The esterase and proteolytic activity of fish proteinases is concentrated in the same active site and reaches the highest values at pH 7,8. New data are presented on particularities of the lower vertebrate proteinases, on the similarity and differences in their specificity. A distinct difference is shown in the nature of the binding site of the active centre in a number of serine proteinases of fishes as compared to chymotrypsin and trypsin of higher vertebrates.
对低等脊椎动物丝氨酸蛋白酶作用的最新数据进行了总结。详细考虑了不同合成底物的水解特异性和动力学、酶活性对pH的依赖性、它们被氨基酸和肽的氯甲基酮以及高分子量蛋白酶抑制剂的不可逆抑制作用。数据证明高等脊椎动物的胰凝乳蛋白酶和胰蛋白酶以及低等脊椎动物的丝氨酸蛋白酶起酸碱催化作用。鱼类幽门盲囊中的酶处于酶原状态，并借助自身的蛋白水解因子转化为活性形式。鱼类蛋白酶的酯酶和蛋白水解活性集中在同一活性位点，在pH 7.8时达到最高值。给出了关于低等脊椎动物蛋白酶特性、其特异性的异同的新数据。与高等脊椎动物的胰凝乳蛋白酶和胰蛋白酶相比，多种鱼类丝氨酸蛋白酶活性中心结合位点的性质存在明显差异。
