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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。
Studies on catalytic functional groups of Actinidin (EC 3,4,22,14) showed that one free thiol group has one histidine residue as an essential group for enzyme catalytic activity. The tryptophan residue is an enzyme activity Performance is necessary; carboxyl and catalytic activity similar. To date, no reports on the role of lysine residues have been reported. In this paper, TNBS (2,4,6-trinitrobenzene sulfonic acid) modified kinetic method and spectroscopic analysis were used to further explore the relationship between lysine residues and Actinidin catalytic activity. The separation and purification of enzyme identification and enzyme activity determination are described in reference [4], other experimental conditions see the legend.