Abstract
The peroxidase activity in the uterine extract of rats previously given a low dose of oestradiol has been examined. From sexually mature rats, two peroxidases of apparent molecular weights of 92 000 (peroxidase I) and 40 000 (peroxidase II) and of different mobilities in polyacrylamide disc gel electrophoresis were found. The two peroxidases were separated and characterized in terms of their substrate specificities, kinetics, pH optima for activity, inhibitors and stabilities. Both enzymes appeared to be classic haemoprotein peroxidases of very similar properties. Peroxidase II was further purified.
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