摘要
通过简便的两步阴离子交换色谱，从遗传工程菌株大肠杆菌JM105中纯化出哺乳动物的谷胱甘肽S-转移酶5－5（GST5－5）．GST5－5以二卤甲烷为底物时的动力学常数、热稳定性和最适pH被测定，并与细菌二氯甲烷脱卤素酶（DM11脱卤素酶）的上述性质进行了比较．
Mammalian glutathione S-transferase 5-5 (GST 5-5) was purified from E. coli strainJM105 in which rat GST 5-5 cDNA was cloned by simple two-step anion-exchange chro-matography. Kinetic constants,heat-stability and pH optimum of the enzyme were deter-mined and compared with bacterial dichloromethane dehalogenase.
出处
《南开大学学报（自然科学版）》
CAS
CSCD
北大核心
1997年第3期76-81,共6页
Acta Scientiarum Naturalium Universitatis Nankaiensis
基金
国家自然科学基金!39670021
关键词
谷胱甘肽
S-转移酶
二氯甲烷
脱卤素酶
热稳定性
glutathione S-transferase 5-5
bacterial dichloromethane dehalogenase
kinetic constants
heat-stability
pH optimum
