嗜热脂肪芽孢杆菌中NADH-（二氯酚靛酚）氧化还原酶的纯化
Purification of an NADH-(dichlorophenol-indophenol) oxidoreductase from Bacillus stearothermophilus.
作者信息
Mains I, Power D M, Thomas E W, Buswell J A
出版信息
Biochem J. 1980 Nov 1;191(2):457-65. doi: 10.1042/bj1910457.
Abstract
An NADH-(dichlorophenol-indophenol) oxidoreductase was purified 104-fold and in 25% overall yield from the thermophilic bacterium Bacillus stearothermophilus, strain PH24. After solubilization in 2M-NaCl at 70 degrees C, the enzyme was purified by ion-exchange and hydroxyapatite chromatography, followed by affinity chromatography on immobilized Cibacron Blue 3GA. The purified enzyme had a mol.wt. of 43 000 and had an absorption spectrum characteristic of flavoprotein. The enzyme activity was enhanced by FMN and by CN-. The enzyme was inhibited by EDTA and by rho-chloromercuribenzoic acid.
摘要
从嗜热脂肪芽孢杆菌PH24菌株中纯化出一种NADH -（二氯酚靛酚）氧化还原酶，纯化倍数为104倍，总产率为25%。在70℃下用2M氯化钠溶解后，该酶通过离子交换和羟基磷灰石色谱法进行纯化，随后在固定化的Cibacron Blue 3GA上进行亲和色谱。纯化后的酶分子量为43000，具有黄素蛋白的吸收光谱特征。FMN和CN -可增强该酶的活性。该酶受到EDTA和对氯汞苯甲酸的抑制。
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