Co-Authors:
Lurie, S., Division of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Ben-Arie, R., Division of Fruit and Vegetable Storage, Agricultural Research Organization, The Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Abstract:
The ATPase found in the 80000g pellet of apple fruit showed a pH optimum of 6, was inhibited by divalent cations and stimulated by monovalent cations. The enzyme was specific for ATP and inhibited by diethylstilbestrol and dicyclohexylcarbodiimide, while unaffected by oligomycin and the uncoupler SF 6874. The Km for ATP was 0.48 mM, Vmax1.2,μmol Pi/mg protein/min. Mg2+ was a competitive inhibitor to ATP; Ki0.7 mM. As the apple ripened from preclimacteric to postclimacteric, the ATPase activity increased more than two-fold. © 1983.
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