Stereoisomeric alanine peptides as substrates for human spleen fibrinolytic proteinase (SFP).
作者:YOSHIO OKADA、YOKO NAGAMATSU、YUKO TSUDA、UTAKO OKAMOTO
DOI:10.1248/cpb.29.1762
日期:——
Four kinds of stereoisomeric Z-Ala-Ala-OMe and eight kinds of stereoisomeric Z-Ala-Ala-Ala-OMe were tested as substrates for human spleen fibrinolytic proteinase (SFP) in comparison with porcine pancreatic elastase. Both enzymes exhibited esterase activity towards not only Z-L-Ala-L-Ala-L-Ala-OMe (VI) but also Z-D-Ala-L-Ala-L-Ala-OMe (VII). The rate of esterolysis of VI by elastase was only about twice the rate of esterolysis by SFP although the rate of amidolysis of Suc-L-Ala-L-Ala-L-Ala-pNA (XVI) by elastase was tenfold faster than that by SFP.
与猪胰弹性蛋白酶相比,本研究测试了作为人脾纤维蛋白溶解酶(SFP)底物的四种立体异构体 Z-Ala-Ala-OMe 和八种立体异构体 Z-Ala-Ala-Ala-OMe。这两种酶不仅对 Z-L-Ala-L-Ala-L-Ala-Ome(VI),而且对 Z-D-Ala-L-Ala-L-Ala-Ome(VII)都表现出酯酶活性。虽然弹性蛋白酶对 Suc-L-Ala-L-Ala-L-Ala-pNA (XVI)的酰胺分解速度是 SFP 的十倍,但弹性蛋白酶对 VI 的酯解速度仅是 SFP 的两倍左右。