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首页> 外文期刊>Preparative biochemistry & biotechnology: An international journal for rapid communication >Purification and some properties of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans
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Purification and some properties of thiosulfate dehydrogenase from Acidithiobacillus ferrooxidans

机译：氧化亚铁硫杆菌中硫代硫酸盐脱氢酶的纯化及部分性质

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摘要

Thiosulfate dehydrogenase was purified from Acidithiobacillus ferrooxidans using three purification steps. The purification procedure involved ammonium sulfate fractionation, ion-exchange chromatography, and gel permeation chromatography. Specific activity of the purified enzyme (after IEC) was 3.26 nkat/mg, and yield of the enzyme was 78%. The purity of the enzyme was checked by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The enzyme is a tetramer composed of four probably identical subunits of relative molecular weight 45,000. The pH optimum of the enzyme reaction in the direction of substrate oxidation was found to be 3.0. The isoelectric point of the enzyme was 8.3. Enzyme activity was found to be particularly sensitive to the histidine-selective reagent diethylpyrocarbonate. Reagents selective for arginine, cysteine, and tryptophane had no effect on enzyme activity.
机译：使用三个纯化步骤从酸性氧化亚铁硫杆菌中纯化硫代硫酸盐脱氢酶。纯化步骤包括硫酸铵分级分离，离子交换色谱和凝胶渗透色谱。纯化的酶的比活度（IEC后）为3.26nkat / mg，酶的产率为78％。在十二烷基硫酸钠存在下，通过聚丙烯酰胺凝胶电泳检查酶的纯度。该酶是由相对分子量45,000的四个可能相同的亚基组成的四聚体。发现在底物氧化方向上酶反应的最适pH为3.0。酶的等电点为8.3。发现酶活性对组氨酸选择性试剂焦碳酸二乙酯特别敏感。对精氨酸，半胱氨酸和色氨酸具有选择性的试剂对酶活性没有影响。

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