摘要
有关中华猕猴桃蛋白酶(Actinidin,E C 3、4.22.14)催化功能基团的研究表明:CYSH—25、His—161为酶活性部位必需基团,而Lys和Trp残基为酶活力表现所必需。本文中报道应用水溶性碳二亚胺(EDC)修饰动力学方法。
Actinidin was isolated and purified from fruits of wild Actinidia chinensis. The enzyme can be repidly inactivated by water-soluble carbodiimide (1-ethy-3-(3-dimethyl aminoprgpyl) carbodi-imide, EDC). The chemical modification kinetic data indicated that only one carboxyl group was related to the enzyme activity.
出处
《厦门大学学报(自然科学版)》
CAS
CSCD
北大核心
1992年第4期452-454,共3页
Journal of Xiamen University:Natural Science
关键词
蛋白酶
羧基
修饰
催化
Modification, Carboxyl group, Actinidin