Tsai C S, Evan S N, Asselberg P J, McGregor R R, Fowler D B
Int J Biochem. 1983;15(11):1321-8. doi: 10.1016/0020-711x(83)90022-8.
Pyruvate kinase has been purified from codfish muscle. The ratio of phosphotransferase and oxalacetate decarboxylase activities remains relatively constant throughout purification steps. These two activities are dependent as well as sensitive to sulfhydryl reagents. In the presence of dithioerythritol, only one molecular form of pyruvate kinase is detected. However, the enzyme exists as four pseudoisozymes in the presence of 2-mercaptoethanol. The pseudoisozymes of codfish pyruvate kinase are interconvertible under the influence of sulfhydryl reagents.
丙酮酸激酶已从鳕鱼肌肉中纯化出来。在整个纯化步骤中，磷酸转移酶和草酰乙酸脱羧酶活性的比率保持相对恒定。这两种活性既相互依赖，又对巯基试剂敏感。在二硫苏糖醇存在的情况下，仅检测到一种分子形式的丙酮酸激酶。然而，在2-巯基乙醇存在的情况下，该酶以四种假同工酶的形式存在。鳕鱼丙酮酸激酶的假同工酶在巯基试剂的影响下可相互转化。
