马铃薯a型磷脂酶的纯化、特性鉴定及其对马铃薯线粒体的影响。
Purification and characterization of an a type phospholipase from potato and its effect on potato mitochondria.
作者信息
Hasson E P, Laties G G
机构信息
Department of Biology and Molecular Biology Institute, University of California, Los Angeles, California 90024.
出版信息
Plant Physiol. 1976 Feb;57(2):148-52. doi: 10.1104/pp.57.2.148.
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 Ca(2+) at pH above 7.5 and inhibited by Ca(2+) 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.
已对一种马铃薯（茄属马铃薯）磷脂酰水解酶进行了纯化和特性鉴定，该酶在pH值7.5至8.5范围内对磷脂的作用效果比对半乳糖脂的作用效果至少高10000倍。它是一种可溶性酶，很容易与中性脂质脂肪酶和第三种脂质酰基水解酶区分开来，后一种酶虽然作用于磷脂，但对甘油单油酸酯表现出明显的偏好。所讨论的磷脂酶的最适pH值为8.5，在pH值高于7.5时受Ca(2+)刺激，在较低pH值时受Ca(2+)抑制，虽然在一定程度上受 Triton X-100刺激，但不依赖于去污剂，并且在接近零的温度下仍保持非常活跃。完整马铃薯线粒体的磷脂极易被马铃薯磷脂酶降解，有人认为这种酶参与了新鲜马铃薯切片切割后发生的广泛脂质分解，以及线粒体在制备和老化过程中的退化。
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