[Peroxidase activity of succinylated catalase].
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.
D000818:Animals; D002374:Catalase / Q000378:metabolism*; D002417:Cattle; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D009195:Peroxidase; D010544:Peroxidases / Q000378:metabolism*; D013387:Succinic Anhydrides / Q000494:pharmacology
D007527:Isoenzymes; D013387:Succinic Anhydrides; D010544:Peroxidases; D002374:Catalase; D009195:Peroxidase
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