Poerio E, Davies D D
Biochem J. 1980 Nov 1;191(2):341-8. doi: 10.1042/bj1910341.
A 2000-fold purification of L(+)-lactate dehydrogenase from potatoes is reported. Five isoenzymes of lactate dehydrogenase can be detected in crude extracts of potato, and three of these are present in the purified preparation. The enzyme (mol.wt. 150 000), which is composed of four subunits (mol.wt. 37 500), is active with the same oxo acids and hydroxy acids that have been reported as substrates with the same oxo acids and hydroxy acids that have been reported as substrates for vertebrate lactate dehydrogenases. These similarities between potato and vertebrate lactate dehydrogenases contrast sharply with some other reports on potato lactate dehydrogenase. These discrepancies are discussed in relation to the proposition that vertebrate and potato lactate dehydrogenases share a common evolutionary origin.
据报道，从土豆中纯化出了2000倍的L(+)-乳酸脱氢酶。在土豆粗提物中可检测到五种乳酸脱氢酶同工酶，其中三种存在于纯化制剂中。该酶（分子量150000）由四个亚基（分子量37500）组成，对与已报道的脊椎动物乳酸脱氢酶底物相同的氧代酸和羟基酸具有活性。土豆和脊椎动物乳酸脱氢酶之间的这些相似性与其他一些关于土豆乳酸脱氢酶的报道形成了鲜明对比。结合脊椎动物和土豆乳酸脱氢酶具有共同进化起源这一观点，对这些差异进行了讨论。
