金属离子对棉铃虫N-乙酰-β-D-氨基葡萄糖苷酶活力的影响  

Effects of Metal Ions on the Activity of β-N-acetyl-D-glucosaminidase from the Pupae of Helicoverpa armigera

作　　者：王君[1] 黄小红[2] 陈清西[1] 

机构地区：[1]厦门大学生命科学学院细胞生物学与肿瘤细胞工程教育部重点实验室,福建厦门361005 [2]福建农林大学生物农药与化学生物学教育部重点实验室,福建福州350002

出　　处：《厦门大学学报（自然科学版）》2005年第6期843-846,共4页Journal of Xiamen University：Natural Science

基　　金：福建省科技攻关课题(2004N002);福建省自然科学基金(B0410003)资助

摘　　要：研究了金属离子对棉铃虫N-乙酰--βD-氨基葡萄糖苷酶(EC3.2.1.52)活力的影响.结果表明:Na+、K+和Li+等金属离子对酶活力没有任何影响;在指定范围内,Mg2+和Ca2+对酶活力影响不显著;Zn2+、Cu2+和Al3+对该酶有不同程度的抑制作用.进一步研究Cu2+和Al3+的抑制作用动力学,结果表明:Cu2+对该酶的抑制作用是一种可逆过程,抑制机理表现为混合型,抑制常数KI为0.23 mmol/L,KIS为1.49 mmol/L.Al3+对该酶的抑制作用是一种可逆过程,抑制机理表现为竞争性类型,抑制常数KI为6.42 mmol/L.The effects of metal ions on β-N-acetyl-D-glucosaminidase （NAGase, EC3. 2.1. 52） from Helicoverpa armigera have been studied. The results show that Na^＋ , K^＋ and Li^＋ ions have no effect on the enzyme activity. Mg^2＋ and Ca^2＋ ions have few effects on the enzyme activity,while Zn^2＋ ,Cu^2＋ and Al^3＋ inhibit the enzyme. The inhibitory kinetics of Cu^2＋ and Al^3＋ on the enzyme was further studied. The results showed that Cu^2＋ was a reversible inhibitor of the enzyme and the inhibition was determined to be of mixed type. The inhibition constants of free enzyme （Kl） and enzyme-substrate complex （K1s） are determined to be 0. 23 mmol/L and 1.49 mmol/L, respectively. Al^3＋ is a reversible competitive inhibitor of the enzyme, and the inhibition constants （Kl） was determined to be 6.42 mmol/L.

关 键 词：N-乙酰-Β-D-氨基葡萄糖苷酶 棉铃虫 金属离子 抑制动力学 

分 类 号：Q356.1[生物学—遗传学]