Fong W P, Chan E Y, Lau K K
Department of Biochemistry, Chinese University of Hong Kong, Shatin, N.T., Hong Kong.
Biochem Mol Biol Int. 1998 Jun;45(2):409-18. doi: 10.1080/15216549800202792.
Two chymotrypsins were purified from the hepatopancreas of grass carp (Ctenopharyngodon idellus) by chromatographies on phenyl-Sepharose and Q-Sepharose. The molecular weights of chymotrypsins I and II were 28 and 27 kDa, respectively. The two chymotrypsins showed similar susceptibility to inhibitions by phenylmethylsulfonyl fluoride and soybean trypsin inhibitor, but differed in their response to tosyl-L-phenylalanine chloromethyl ketone and aprotinin in which chymotrypsin I was more resistant. Chymotrypsin I was a less typical chymotrypsin and exhibited lower catalytic efficiency with the chymotrypsin-specific ester and amide substrates, when compared with chymotrypsin II. For both chymotrypsins, optimal activity was detected in the pH range 7.0-8.5.
通过在苯基琼脂糖和Q-琼脂糖上进行色谱分离，从草鱼（Ctenopharyngodon idellus）的肝胰腺中纯化出两种胰凝乳蛋白酶。胰凝乳蛋白酶I和II的分子量分别为28 kDa和27 kDa。这两种胰凝乳蛋白酶对苯甲基磺酰氟和大豆胰蛋白酶抑制剂的抑制作用表现出相似的敏感性，但对甲苯磺酰-L-苯丙氨酸氯甲基酮和抑肽酶的反应不同，其中胰凝乳蛋白酶I更具抗性。与胰凝乳蛋白酶II相比，胰凝乳蛋白酶I是一种不太典型的胰凝乳蛋白酶，对胰凝乳蛋白酶特异性酯和酰胺底物的催化效率较低。对于这两种胰凝乳蛋白酶，在pH 7.0 - 8.5范围内检测到最佳活性。
