Purification and Some Properties of Bilirubin Oxidase of Myrothecium verrucaria MT-1
Purification and Some Properties of Bilirubin Oxidase of Myrothecium verrucaria MT-1
复制标题
疣状漆斑菌MT-1胆红素氧化酶的纯化及部分性质
DOI：
10.1271/bbb1961.46.2499
复制
发表时间：
1982
期刊：
影响因子：
--
通讯作者：
S. Murao
中科院分区：
文献类型：
--
作者：
N. Tanaka;S. Murao
采用硫酸铵沉淀、活性炭处理、QAE-Sephadex A-50和Sephadex G-100柱层析等方法，从疣孢漆斑菌MT-1培养滤液中分离纯化了胆红素氧化酶。纯化后的酶经盘状凝胶电泳显示均一性，酶中含有铜和碳水化合物。该酶被Fe ~（2+）和与铜络合的化合物抑制。该酶能氧化胆红素、胆绿素、氯化血红素和叶绿酸等四吡咯化合物及漆酶底物。胆红素比其他物质氧化更快。胆红素氧化酶与漆酶的反应性不同，它与四吡咯组成的物质反应。由四吡咯组成的物质仅被漆酶少量氧化，但被胆红素氧化酶迅速氧化。胆红素的表观Km值计算为190 μm。
Bilirubin oxidase was purified from the culture filtrate of Myrothecium verrucaria MT-1 by a procedure involving ammonium sulfate precipitation, charcoal treatment, and QAE-Sephadex A-50 and Sephadex G-100 column chromatographies. The purified enzyme was homogeneous on disc gel electrophoresis.Copper and carbohydrate were contained in the enzyme. The enzyme was inhibited by Fe2+ and compounds that complex with copper. Bilirubin, biliverdin, hemin and chlorophyllin which consist of tetrapyrrole, and substrates of laccase were oxidized by the enzyme. Bilirubin was oxidized more rapidly than other substances. Bilirubin oxidase differed from laccase in reactivity with substances consisting of tetrapyrrole. Substances consisting of tetrapyrrole were oxidized only a little by laccase but rapidly oxidized by bilirubin oxidase. The apparent Km value for bilirubin was calculated to be 190 μm.