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Purification and Characterization of an A Type Phospholipase from Potato and Its Effect on Potato Mitochondria ^1,2

^a Department of Biology and Molecular Biology Institute, University of California, Los Angeles, California 90024

A potato (Solanum tuberosum) phospholipid acyl-hydrolase, which - in the pH range 7.5 to 8.5—is at least 10,000 times more effective with phospholipids than with galactolipids, has been purified and characterized. It is a soluble enzyme readily distinguished from a neutral lipid lipase and a third lipid acyl-hydrolase which, while acting on phospholipid, shows a decided preference for glyceryl monoolein. The phospholipase in question has a pH optimum of 8.5, is stimulated by Ca²⁺ at pH above 7.5 and inhibited by Ca²⁺ at lower pH, is not dependent on detergents although stimulated by Triton X-100 to a moderate extent, and remains very active at temperatures close to zero. The phospholipids of intact potato mitochondria are highly susceptible to degradation by potato phospholipase, and it is suggested that this enzyme is involved in the extensive lipid breakdown which occurs in fresh potato slices following cutting, and in the deterioration of mitochondria during their preparation and aging.

² In honor of Leon Bernstein—warm friend, dedicated plant physiologist, and devoted editor.

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