Abstract
A procedure involving vigorous blending of protein preparations has been developed for the separation of an endogenous macromolecular inhibitor from potato invertase. The resultant foaming completely destroys the inhibitor but does not inactivate the enzyme. Application of this technique revealed that invertase in potato tubers is always detectable but is present in highest levels in tubers stored at low temperatures. A marked decrease in invertase and a concomitant increase in inhibitor occur when tubers are transferred from cold to warm storage. Both the enzyme and its inhibitor have been partially purified. Optimal invertase activity was shown to occur at pH 4.7. Addition of purified inhibitor to invertase produces non-competitive inhibition. The inhibitor is most effective at the pH optimum for invertase and its presence results in double pH optima.
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