抄録
1. It was shown that the IAA oxidase activity in wheat germ was solely attributed to the peroxidases isolated by the present authors. The IAA oxidase activity was divided into two activities, an “Acidic IAA Oxidase Activity” and a “Neutral IAA Oxidase Activity”.
2. The neutral IAA oxidase activity of peroxidase 566 had the pH optimum at 6.4 and was stimulated by 10-5M of manganese ion and inhibited by the larger amount of it. Catalase inhibited the activity.
3. The acidic IAA oxidase activity of peroxidase 556 had the pH optimum at 4.0 and was stimulated remarkably by 10-2M of manganese ion. Lower concentrations of manganese ion also stimulated the activity. Peroxidase 556 was inactive at neutral pH's.
The authors express their many thanks to Prof. Okunuki, K. for his guidance and encouragement during the work, to Prof. Hagihara, B. for analysis of oxygen consumption and his advice and to Dr. Ito, T. for his helpful discussion for the work.
