Northeastern Forest Experiment Station, Forest Service, United States Department of Agriculture, Durham, New Hampshire 03824.
Plant Physiol. 1972 Jul;50(1):15-8. doi: 10.1104/pp.50.1.15.
The isolation of a unique enzyme capable of oxidizing indoleacetic acid, but devoid of peroxidase activity, has been reported for preparations from tobacco roots and commercial horseradish peroxidase. Experiments were made to verify these results using enzyme obtained from Betula leaves and commercial horseradish peroxidase. Both indoleacetic acid oxidase and guaiacol peroxidase activity appeared at 2.5 elution volumes from sulfoethyl-Sephadex. These results were obtained with both sources of enzyme. In no case was a separate peak of indoleacetic acid oxidase activity obtained at 5.4 elution volumes as reported for the tobacco enzyme using the same chromatographic system. Both types of activity, from both sources of enzyme, also eluted together during gel filtration. Successful column chromatography of Betula enzyme was dependent upon previous purification by membrane ultrafiltration. These results indicate indoleacetic acid oxidase activity and guaiacol peroxidase activity are dual catalytic functions of a single enzyme.
已从烟草根和商业辣根过氧化物酶制剂中分离出一种能够氧化吲哚乙酸但缺乏过氧化物酶活性的独特酶。使用桦树叶和商业辣根过氧化物酶获得的酶进行了实验以验证这些结果。从 sulfoethyl-Sephadex 洗脱 2.5 个洗脱体积时，出现了吲哚乙酸氧化酶和愈创木酚过氧化物酶活性。这两个来源的酶都得到了相同的结果。在任何情况下，都没有像使用相同的色谱系统报告的烟草酶那样，在 5.4 个洗脱体积处获得吲哚乙酸氧化酶活性的单独峰。两种类型的酶，无论是来自哪种来源，在凝胶过滤时也一起洗脱。桦树酶的成功柱层析取决于之前通过膜超滤进行的纯化。这些结果表明，吲哚乙酸氧化酶活性和愈创木酚过氧化物酶活性是单一酶的双重催化功能。
