【摘要】 <正> 有关中华猕猴桃蛋白酶(Actinidin,EC 3,4,22,14)催化功能基团的研究表明一个游离巯基,一个组氨酸残基为酶催化活性中心必需基团;色氨酸残基为酶活力表现所必需;羧基似与催化活性有关。迄今尚未见到有关赖氨酸残基作用的报道。本文应用TNBS(2,4,6-三硝基苯磺酸)修饰动力学方法和光谱分析,进一步探讨了赖氨酸残基与Actinidin催化活性之间的关系。有关酶的分离提纯鉴定及酶活力测定均参照文[4],其它实验条件见图注。更多还原

【Abstract】 Actinidin was isolated and purified from fruits of wild Actinidio chi-nensis. The enzyme can be rapidly inactivated by amino group regent, 2, 4, 6-trinitrobenzene sulfonatc (TNBS). Spectrum analysis for TNBS inactivated enzyme showed that lysine residues of the enzyme were modified by TNBS. The chemical modification kinetic data indicated that only one lysine resi-due was related to the enzyme activity.更多还原