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Articles

ATP-Dependent Proteolytic Activity from Spinach Leaves ¹

Department of Biochemistry and Biophysics, University of California, Davis, California 95616

Spinach (Spinacia oleracea CV Bloomsdale Long Standing) leaf cytoplasmic starch phosphorylase and rabbit muscle phosphorylase a were inactivated by incubation with partially purified leaf extract in the presence of ATP and Mg²⁺. The inactivating factor(s) were heat stable and susceptible to protease attack. Phosphorylase inactivation was prevented by incubation in the presence of p-aminobenzamidine and phenylboronic acid, or prolonged treatment with phenylmethylsulfonyl fluoride or leupeptin for the ATP-stimulated inhibitory activity. Mg²⁺ -dependent inactivation was prevented by incubation with leupeptin, phenylmethylsulfonyl fluoride, p-aminobenzamidine, or 5'-adenylate. ATP-mediated inactivation of phosphorylase was stimulated by Mg²⁺ with a reduction in the apparent K_m for ATP. Casein-degrading activities with the same properties of ATP and/or Mg²⁺ stimulation, heat stability, and susceptibility to proteinase inhibitors were detected suggesting that phorphorylase inactivation was due to proteolysis. The activity was greatest at about the time of flowering and also appeared to depend on the light regime.

¹ The research reported herein was supported in part by National Science Foundation Grants PCM 78-16127 and PCM 82-05705.