Cs-Szabó G, Széll E, Elödi P
FEBS Lett. 1986 Jan 20;195(1-2):265-8. doi: 10.1016/0014-5793(86)80173-9.
The kinetic features of human granulocyte elastase, chymotrypsin, porcine pancreatic elastase and elastomucoproteinase were compared. Amino acyl ester substrates were assayed and Km and kcat values were defined. Aldehyde analogues of the p-nitroanilide substrates designed for granulocyte elastase as optimal for Km appeared to be potent inhibitors. Suc-D-Phe-Pro-valinal (Ki = 40 microM) was found to inhibit granulocyte elastase competitively and specifically when measured with synthetic substrates, and the Ki was 3 microM with the natural protein substrate, elastin.
比较了人粒细胞弹性蛋白酶、胰凝乳蛋白酶、猪胰弹性蛋白酶和弹性粘蛋白酶的动力学特征。对氨酰酯底物进行了测定，并确定了Km和kcat值。为粒细胞弹性蛋白酶设计的对硝基苯胺底物的醛类似物，对Km而言似乎是最佳的，它们是有效的抑制剂。当用合成底物进行测定时，发现琥珀酰-D-苯丙氨酸-脯氨酸-缬氨酸醛（Ki = 40 microM）竞争性且特异性地抑制粒细胞弹性蛋白酶，而对于天然蛋白质底物弹性蛋白，其Ki为3 microM。
