Davies D D, Asker H
Station de Physiologie Végétale, Institut National de la Recherche Agronomique, La Grande Ferrade, 33140 Pont-de-la-Maye, Bordeaux, France.
Plant Physiol. 1983 May;72(1):134-8. doi: 10.1104/pp.72.1.134.
A rapid purification of lactate dehydrogenase and glycolate oxidase from lettuce (Lactuca sativa) leaves is described. The kinetics of both enzymes are reported in relation to their possible roles in the production of oxalate. Lettuce lactate dehydrogenase behaves like mammalian dehydrogenase, catalyzing the dismutation of glyoxylate to glycolate and oxalate. A model is proposed in which glycolate oxidase in the peroxisomes and lactate dehydrogenase in the cytosol are involved in the production of oxalate. The effect of pH on the balance between oxalate and glycolate produced from glyoxylate suggests that in leaves lactate dehydrogenase may function as part of an oxalate-based biochemical, pH-stat.
本文描述了从生菜（莴苣）叶片中快速纯化乳酸脱氢酶和乙醇酸氧化酶的方法。报道了这两种酶的动力学与其在草酸盐产生中可能发挥的作用之间的关系。生菜乳酸脱氢酶的行为类似于哺乳动物脱氢酶，催化乙醛酸歧化为乙醇酸和草酸盐。提出了一个模型，其中过氧化物酶体中的乙醇酸氧化酶和细胞质中的乳酸脱氢酶参与草酸盐的产生。pH对乙醛酸产生的草酸盐和乙醇酸之间平衡的影响表明，在叶片中乳酸脱氢酶可能作为基于草酸盐的生化pH稳态的一部分发挥作用。
