鯨スイ臓のタンパク分解酵素に関する研究-4-長須鯨スイ臓カチオニック・トリプシンの性質について〔英文〕(速報)

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The properties of isolated and purified fin whale trypsin were studied and compared with those of bovine trypsin. S20, w was 2.3 S and its molecular weight was determined as 17, 000. The optimum pH ranged between 7.5 and 8.0 in the case of casein as substrate, while it was 7.5 in the case of BAEE. The specific activity was almost similar to that of bovine trypsin toward casein as substrate, but was half as much as that of bovine trypsin toward BAEE. The enzyme was inhibited by DFP and TLCK, and reacted stoichiometrically at the ratio of one mole to one mole of ovomucoid and soybean trypsin inhibitor, respectively. Unlike bovine trypsin, fin whale trypsin was considerably stable at neutral and weak alkaline pH. It was rather similar to porcine trypsin.