链状亚历山大藻谷氨酰胺合成酶的分离纯化及酶学特性研究  

Purification and characterization of glutamine synthetase from Alexandrium catenella

作　　者：丁光茂[1] DING Guangmao(Ocean Environment and Fishery Resources Monitoring Center of Fujian Province,Fuzhou 350003,China)

机构地区：[1]福建省海洋环境与渔业资源监测中心,福建福州350003

出　　处：《渔业研究》2018年第2期98-103,共6页Journal of Fisheries Research

基　　金：国家重点研发计划(2017YFC1404800);海洋公益性行业科研专项(No.201205009)

摘　　要：本文以链状亚历山大藻(Alexandrium catenella)为实验材料,通过离子交换、分子筛和疏水层析等纯化技术来分离纯化谷氨酰胺合成酶(Glutamine synthetase,GS),并对GS的理化特性进行研究。研究结果表明,GS分子量为430 kD,由8个分子量为55.6 kD的亚基组成;按照亚基分子量的大小判断,链状亚历山大藻GS属于GSⅠ类型。GS反应的最适pH和温度分别为8.0和25℃,Mg^(2+)离子参与的GS反应,GS活力表达最高,Cu^(2+)、K+、Zn^(2+)、Ni^(2+)、Ca^(2+)、Ce^(2+)、Mn^(2+)对GS活力均有一定的抑制作用,Fe^(2+)和Fe^(3+)则完全抑制了GS活力。The crude glutamine synthetase(GS)precipitated by streptomycin sulphate from Alexandrium catenella was purified after subsequently passing through ion-exchange chromatography,Gel-filtration Sephacry1 S-300 and Phenyl-sepharose CL-4B.The molecular weight of GS was 430 kD,which consisted of 8 subunits with molecular weight of 55.6 kD.GS purified from Alexandrium catenella belonged to GSⅠ.The optimal pH and temperature of maximal GS activity were 8.0 and 25℃,respectively.The presence of Mg 2+resulted in the highest GS activity,while GS activity was fully inhibited in the presence of Fe 2+and Fe 3+.

关 键 词：谷氨酰胺合成酶(GS) 离子交换柱 分子筛 

分 类 号：P735[天文地球—海洋生物学]