Trommer W E, Becker G
Biochim Biophys Acta. 1976 Jan 23;422(1):1-7. doi: 10.1016/0005-2744(76)90002-4.
Pig heart lactate dehydrogenase (L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) was partially inactivated by reaction with phenylmaleimide. The resulting protein mixture was separated by affinity chromatography on a Sepharose-linked oxamate column yielding three distinct enzyme fractions with one, two and three out of four subunits being modified. The specific activities of these samples were lower than expected from the degree of modification, while the maximum binding capacity of NADH-oxamate related well to the number of catalytic centers modified. A possible cooperative effect in the native enzyme is discussed.
猪心乳酸脱氢酶（L-乳酸：NAD+氧化还原酶，EC 1.1.1.27）与苯基马来酰亚胺反应后部分失活。所得蛋白质混合物通过在琼脂糖连接的草氨酸盐柱上进行亲和层析分离，得到三个不同的酶组分，其四个亚基中的一个、两个和三个被修饰。这些样品的比活性低于根据修饰程度预期的值，而NADH-草氨酸盐的最大结合能力与被修饰的催化中心数量密切相关。文中讨论了天然酶中可能存在的协同效应。
