化学修饰实验发现：巯基、胍基、氨基、羧基和吲哚基可能参与酶活性中心的组成。
Chemical modification studies showed that the sulfhydryl, guanido, amino, carboxyl and indolyl groups may participate in the active center of the enzyme.
本文用各种化学修饰剂对脱卤酶yl、109和H - 2进行化学修饰。
Chemical modification reactions of dehalogenase YL, 109 and H-2 were carried out by various reagents.
重点讨论了脂肪酶的化学修饰，尤其是在修饰方法和修饰机理方面的研究进展。
Highlights were given to the developments of chemical modification which focusing on the modification methods and activation mechanism.
运用化学修饰方法对一株嗜热芽孢杆菌所产生的耐高温蛋白酶hs08活性中心的结构进行了研究。
Chemical modification of amino acid side chain groups on protease HS08 secreted by a thermophilic Bacillus strain were investigated.
化学修饰法研究进一步证明侧链羧基是酶的必需基团，并测定出酶活性必需的羧基数为一个。
These results showed that the ionizing group of the enzyme active center is the carboxyl group.
化学修饰法研究进一步证明侧链羧基是酶的必需基团，并测定出酶活性必需的羧基数为一个。
These results showed that the ionizing group of the enzyme active center is the carboxyl group.
应用推荐