Abstract
1. 1. Phosphoenolpyruvate carboxykinases from rat-liver and from the tapeworm Hymenolepis diminuta were compared with respect to metal-ion activation, nucleotide specificity, kinetic parameters and inhibition. 2. 2. Quinolinate and 3-mercaptopicolinate inhibited both enzymes, competitively with phosphoenolpyruvate. 3. 3. Crude rat enzyme, but not crude helminth enzyme, contained carboxykinase ferroactivator which protected the enzyme from inactivation by Fe 2+. Rat-liver ferroactivator protected the helminth enzyme. 4. 4. The two enzymes were similar, but the helminth enzyme showed stronger affinity for metal-ions, phosphoenolpyruvate and inhibitors.
Published Version
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