Tezuka T, Tonomura K
J Bacteriol. 1978 Jul;135(1):138-43. doi: 10.1128/jb.135.1.138-143.1978.
An enzyme (splitting enzyme 2) which catalyzes the splitting of carbon-mercury linkage of arylmercury compounds was found in extracts of mercury-resistant Pseudomonas K-62. This enzyme was purified about 725-fold by treatment with streptomycin, precipitation with ammonium sulfate, and successive chromatography on Sephadex G-75 and diethylaminoethyl-cellulose. A purified preparation of the enzyme showed a single band in electrophoresis either on polyacrylamide or sodium dodecyl sulfate-containing polyacrylamide gels. The molecular weight of the enzyme was estimated to be 20,000 (determined by Sephadex G-75 gel filtration) 17,000 (determined by sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis). The enzyme showed a Km of 180 micron and a Vmax of 3.1 mumol/min per mg for p-chloromercuribenzoic acid and a Km of 250 micron and a Vmax of 20 mumol/min per mg for phenylmercuric acetate. The optimum temperature and pH for the reaction were 40 degrees C and 5.0, respectively.
在抗汞假单胞菌K - 62的提取物中发现了一种能催化芳基汞化合物碳 - 汞键断裂的酶（裂解酶2）。通过用链霉素处理、硫酸铵沉淀以及先后在葡聚糖凝胶G - 75和二乙氨基乙基纤维素上进行层析，该酶被纯化了约725倍。纯化后的酶制剂在聚丙烯酰胺凝胶或含十二烷基硫酸钠的聚丙烯酰胺凝胶电泳中均显示出一条带。通过葡聚糖凝胶G - 75凝胶过滤法测定该酶的分子量估计为20,000，通过十二烷基硫酸钠 - 聚丙烯酰胺圆盘凝胶电泳法测定为17,000。该酶对对氯汞苯甲酸的Km值为180微摩尔，Vmax为每毫克3.1微摩尔/分钟，对醋酸苯汞的Km值为250微摩尔，Vmax为每毫克20微摩尔/分钟。该反应的最佳温度和pH分别为40℃和5.0。
