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

›› 2018, Vol. 40 ›› Issue (2): 98-103.

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

丁光茂

福建省海洋环境与渔业资源监测中心

收稿日期:2018-02-28 修回日期:2018-03-14 出版日期:2018-04-25 发布日期:2018-04-25
通讯作者: 丁光茂
基金资助:
区域海洋生态环境立体监测系统集成与应用示范

Purification and characterization of glutamine synthetase from Alexandrium catenella

ding guangmao

Received:2018-02-28 Revised:2018-03-14 Online:2018-04-25 Published:2018-04-25
Contact: ding guangmao

摘要/Abstract

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℃，Mg2+离子参与的GS反应，GS活力表达最高，Cu2+、K+、Zn2+、Ni2+、Ca2+、Ce2+、Mn2+对GS活力均有一定的抑制作用，Fe2+ 和Fe3+则完全抑制了GS活力。

关键词: 谷氨酰胺合成酶（GS）, 离子交换柱, 分子筛, glutamine sythetase, ion-exchange chromatography, Gel-filtration

Abstract: 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 Mg2+ resulted in the highest GS activity, while GS activity was fully inhibited in the presence of Fe2+ and Fe3+.

中图分类号:

p714+.5

丁光茂. 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[J]. , 2018, 40(2): 98-103.

ding guangmao. Purification and characterization of glutamine synthetase from Alexandrium catenella[J]. , 2018, 40(2): 98-103.