Abstract
Two peroxidase isoenzymes, purified from extracts of Spring cabbage, have been shown to possess different heat-stabilities. The anionic isoenzyme had an isoelectric point of 3·7 and was relatively heat stable, while the cationic isoenzyme, pI 9·9, was more readily inactivated by heat. Neither isoenzyme showed regeneration of peroxidase activity following heat inactivation.
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