Isolation and purification of glutathione peroxidase

被引：6
|
作者：
Shulgin, K. K. [1 ]
Popova, T. N. [1 ]
Rakhmanova, T. I. [1 ]
机构：
[1] Voronezh State Univ, Voronezh 394006, Russia
来源：
APPLIED BIOCHEMISTRY AND MICROBIOLOGY | 2008年 / 44卷 / 03期
关键词：
D O I：
10.1134/S0003683808030034
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Electrophoretically homogeneous glutathione peroxidase (EC 1.11.1.9) preparation from rat liver with a specific activity of 1.46 U/mg of protein and a yield of 7.2% was obtained using the purification procedure developed. The K-M values for reduced glutathione and hydrogen peroxide were 0.033 and 0.208 mM, respectively. The enzymatic reaction had the following characteristics: the temperature optimum, 32 degrees C; the pH optimum, 7.4; and the activation energy, 29.1 kJ/mol. The molecular weight of the enzyme was 88 kDa.
引用
收藏
页码：247 / 250
页数：4
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