Gorecki M, Wilchek M, Blumberg S
Biochim Biophys Acta. 1978 Jul 21;535(1):90-9. doi: 10.1016/0005-2795(78)90036-3.
alpha--Chymotrypsin was modified with three different diazonium salts derived from D--phenylalanine. All three reagents react selectively with tyrosine 146 on the surface of the enzyme. The spectral and enzymatic properties of the azochymotrypsins are characteristic for each of the proteins. Dependent on the structure of the reagent employed for modification, the activity towards rho-nitroanilide substrate can be higher or about the same as that of the native enzyme.
α-胰凝乳蛋白酶用三种源自D-苯丙氨酸的不同重氮盐进行了修饰。所有这三种试剂都能与酶表面的酪氨酸146选择性反应。偶氮胰凝乳蛋白酶的光谱和酶学性质对每种蛋白质来说都是独特的。根据用于修饰的试剂结构，对ρ-硝基苯胺底物的活性可能高于天然酶，也可能与天然酶大致相同。
