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根据邹氏的酶活性不可逆改变动力学理论,我们创建一种测定微观动力学参数方法判断底物对酶活力是否有保护作用,这对阐明酶的空间结构与功能、酶构象变化与活力变化的关系具有重要的科学意义,应用此法判断猕猴桃蛋白酶(Actinidin)在4mol/l盐酸胍和8mol/l脲的失活底物保护是否存在,实验结果表明:1)Actinidin在4mol/l盐酸胍失活过程受到底物一定程度的保护,2)Actindin在8mol/l脲失活过程底物对它完全保护.以上结果也提示了胍、脲作用机制不尽相同。
According to Zou’s theory of irreversible changes in enzyme kinetics, we established a method of determining microscopic kinetic parameters to determine whether a substrate has a protective effect on enzyme activity, which is important for clarifying the spatial structure and function of enzymes, conformational changes and changes in enzyme activity The relationship between Actinidin and 4-deoxyguanidine hydrochloride in the presence of 4mol / l guanidine hydrochloride and 8mol / l urea was investigated. The results showed that: 1) The live process is protected to some extent by the substrate, and 2) Actindin completely protects the substrate from inactivation with 8 mol / l urea.The above results also suggest that guanidine and urea exert different mechanisms.