[牛胰蛋白酶和太平洋鲑鱼胰蛋白酶活性位点结构的比较研究]
[Comparative study of active site structure in bovine and Pacific salmon trypsins].
作者信息
Taran L D, Samus N V
出版信息
Ukr Biokhim Zh (1978). 1994 May-Jun;66(3):49-54.
The kinetic investigation was carried out on the inhibition of hydrolysis of N, alpha-benzoyl-D, L-arginine-p-nitroanilide (BApNA) for bovine and salmon trypsin by phenylmethanesulphonyl fluoride (PMSF), N, alpha-tosyl-L-lysine chloromethyl ketone (N-TLCK), N, alpha-tosyl-L-phenylalanine chloromethyl ketone (N-TPCK). Kinetic parameters of inhibition (Ki, k2) by PMSF for salmon and bovine trypsin differ insignificantly. The k2/Ki value of N-TPCK for salmon trypsin is 10 times more than of bovine trypsin. Kinetic parameters of inhibition by N-TLCK had the less difference. The Ki value of this inhibitor for salmon trypsin is 5 times less than that of bovine trypsin and k2 value is 1.7 times less.
采用苯甲基磺酰氟（PMSF）、N-α-对甲苯磺酰-L-赖氨酸氯甲基酮（N-TLCK）、N-α-对甲苯磺酰-L-苯丙氨酸氯甲基酮（N-TPCK）对牛胰蛋白酶和鲑鱼胰蛋白酶抑制N，α-苯甲酰-D，L-精氨酸对硝基苯胺（BApNA）水解的情况进行了动力学研究。PMSF对鲑鱼胰蛋白酶和牛胰蛋白酶的抑制动力学参数（Ki、k2）差异不显著。N-TPCK对鲑鱼胰蛋白酶的k2/Ki值是牛胰蛋白酶的10倍。N-TLCK的抑制动力学参数差异较小。该抑制剂对鲑鱼胰蛋白酶的Ki值比牛胰蛋白酶低5倍，k2值低1.7倍。
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