Artemchik V D, Kurchenko V P, Metelitsa D I
Biokhimiia. 1985 Jul;50(7):1183-8.
The catalase succinylation by succinic anhydride excess results in an almost complete dissociation of the enzyme into subunits possessing no catalase activity. The catalase subunits show the peroxidatic activity on o-dianisidine oxidation. The oxidation kinetics of this substrate by the succinylated enzyme was studied at various temperatures. The activation energy for this process is 10.1 kcal/mole. Within the temperature range of 31-65.5 degrees, the succinylated enzyme thermostability was studied by monitoring the peroxidatic activity decrease upon o-dianisidine oxidation. The activation energy for the succinylated catalase thermoinactivation equals to 15.5 kcal/mole. The peroxidatic activity of catalase subunits obtained by enzyme succinylation and acidic solution treatment was compared to that of horseradish peroxidase in the oxidation of the same substrate, i.e., o-dianisidine.
过量琥珀酸酐使过氧化氢酶琥珀酰化,导致该酶几乎完全解离成不具有过氧化氢酶活性的亚基。过氧化氢酶亚基在邻联茴香胺氧化反应中表现出过氧化物酶活性。在不同温度下研究了琥珀酰化酶对该底物的氧化动力学。此过程的活化能为10.1千卡/摩尔。在31 - 65.5摄氏度温度范围内,通过监测邻联茴香胺氧化时过氧化物酶活性的降低来研究琥珀酰化酶的热稳定性。琥珀酰化过氧化氢酶热失活的活化能等于15.5千卡/摩尔。将通过酶琥珀酰化和酸性溶液处理得到的过氧化氢酶亚基在相同底物(即邻联茴香胺)氧化反应中的过氧化物酶活性与辣根过氧化物酶的活性进行了比较。