Purification and Properties of L-Cysteine Synthetase from Pseudomonas
- VernacularTitle:假单胞菌L-半胱氨酸合成酶的纯化和性质研究
- Author:
Yong-Jie JIN
;
Wen-Bo YANG
;
Zhong LIU
;
Gang BAI
;
Yang-Sheng YU
;
- Publication Type:Journal Article
- Keywords:
L-ATC hydrolase,L-SCC amidohydrolase,Purification of enzyme,Properties of enzyme
- From:
Microbiology
1992;0(06):-
- CountryChina
- Language:Chinese
-
Abstract:
The L-ATC hydrolase and L-SCC amidohydrolase which convert L-ATC to L-cysteine in Pseudomonas sp.TS-1138 are purified about 83.9 and 90.3 fold by salting-out method, Sephadex G-75 gel chromatography, DEAE-cellulose 52 ion exchange and Sephadex G-100 gel chromatography, etc. The purified enzyemes are both demonstrated by SDS-PAGE to be a homogeneous protein. Their molecular weight are about 37.5kD and42.8kDa respectively. The optimum reaction temperature are both 35℃, and the optimum pH are 7.0 and 8.0 respectively. The Km of the two enzymes are 0.67 mmol/L and 0.15 mmol/L, and the Vmax are 0.39?10 -3mmol/L?min and 0.42?10 -3mmol/L?min respectively.
