Rivoal J, Ricard B, Pradet A
Institut National de la Recherche Agronomique, Station de physiologie Végétale, BP 131, 33140 Pont-de-la-Maye, France.
Plant Physiol. 1991 Mar;95(3):682-6. doi: 10.1104/pp.95.3.682.
A lactate dehydrogenase activity is present in rice (Oryza sativa L.) seedlings and roots. Under aerobic conditions, lactate dehydrogenase activity is barely detectable in rice seedlings and is very low in rice roots. In 30 day old roots, the activity is increased two to three times by an anoxic or hypoxic treatment and can be detected on immunoblots by an antiserum raised against barley lactate dehydrogenase. The activity present in aerobic seedlings was partially purified. The native enzyme has a molecular mass of 160 kilodaltons, and is a tetramer of 2 subunit (38 and 39 kilodaltons) randomly associated. Studies of substrate specificity, native gel electrophoresis, and immunoblot analysis indicate that the partially purified enzyme is a typical lactate dehydrogenase. However, no increase of lactate dehydrogenase activity or protein was observed in seedlings transferred to anoxia.
水稻（Oryza sativa L.）幼苗和根中存在乳酸脱氢酶活性。在有氧条件下，水稻幼苗中几乎检测不到乳酸脱氢酶活性，而在水稻根中该活性非常低。在30日龄的根中，通过缺氧或低氧处理，该活性增加两到三倍，并且可以通过针对大麦乳酸脱氢酶产生的抗血清在免疫印迹上检测到。对有氧幼苗中存在的该活性进行了部分纯化。天然酶的分子量为160千道尔顿，是由两种亚基（38和39千道尔顿）随机结合形成的四聚体。对底物特异性、天然凝胶电泳和免疫印迹分析的研究表明，部分纯化的酶是一种典型的乳酸脱氢酶。然而，转移到缺氧环境中的幼苗中未观察到乳酸脱氢酶活性或蛋白质的增加。
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