Synthesis of chromogenic substrates specific for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE).
作者:YOSHIO OKADA、YUKO TSUDA、AKIO HIRATA、YOKO NAGAMATSU、UTAKO OKAMOTO
DOI:10.1248/cpb.30.4060
日期:——
Various peptide anilides were synthesized by a conventional method with the object of obtaining specific substrates for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE) in order to compare the substrate specificity of SFP with that of LE. It was found that the P1 Val compound among succinyl tripeptide p-nitroanilides (Suc-Tyr-Leu-X-pNA) exhibited the highest kcat/Km values for hydrolysis by SFP and LE, however, the tetrapeptide Suc-Ala-Tyr-Leu-Val-pNA [kcat/Km values (M-1S-1) for hydrolysis by SFP and LE : 84000 and 48000, respectively] was the preferred chromogenic substrate for SFP and LE because of its high solubility in the buffer and its moderate kcat/Km values. The substrate specificity of SFP was found to be similar to that of LE.
通过常规方法合成了多种肽苯胺,目的是获得人类脾纤维蛋白溶解酶(SFP)和人类白细胞弹性蛋白酶(LE)的特定底物,以便比较SFP和LE的底物特异性。研究发现,琥珀酰三肽对硝基苯胺(Suc-Tyr-Leu-X-pNA)中的P1 Val化合物在SFP和LE的水解反应中表现出最高的kcat/Km值,然而,四肽Suc-Ala-Tyr-Leu-Val-pNA(SFP和LE的水解反应的kcat/Km值(M-1S-1):分别为84000和48000)是SFP和LE的首选显色底物,因为它具有在缓冲液中的高溶解性和适中的kcat/Km值。发现SFP的底物特异性与LE的相似。