1970 年 90 巻 10 号 p. 1262-1266
Appropriate working conditions have been studied to separately determine α-chymotrypsin and trypsin in a preparation which is used as an anti-inflamatory enzyme. Soybean trypsin inhibitor (STI) was used as the inhibitor. Trypsin activity in the preparation was completely inhibited by 8×10-3% (w/v) of STI in the reaction system. α-Chymotrypsin activity was partially inhibited and the value of remaining activity was 54.9±3.5%. Thus, it was possible to determine α-chymotrypsin and trypsin activity separately with 8×10-3% of STI. The reaction between trypsin and STI was nearly stoichiometric even in the presence of casein, a substrate. The determination was little affected by most of diluents and binders.