鲟鱼肌肉丙酮酸激酶的纯化及性质
Purification and properties of the pyruvate kinase of sturgeon muscle.
作者信息
Randall R F, Anderson P J
出版信息
Biochem J. 1975 Mar;145(3):569-73. doi: 10.1042/bj1450569.
Abstract
Pyruvate kinase was purified from sturgeon muscle in yeilds comparable with those obtained from the muscles of other species. In contrast with mammalian muscle pyruvate kinase the enzyme from sturgeon muscle gives a sigmoidal velocity curve with respect to phosphoenolpuruvate saturation, is activated by fructose 1.6-diphosphate, and is inhibited by bivalent copper ions. In these respects it is similar to the enzyme isolated from mammalian liver. The degree of interaction between phosphoenolpyruvate-binding sites is dependent on temperature.
摘要
丙酮酸激酶是从鲟鱼肌肉中纯化得到的，其产量与从其他物种肌肉中获得的产量相当。与哺乳动物肌肉丙酮酸激酶不同，鲟鱼肌肉中的这种酶在磷酸烯醇丙酮酸饱和时呈现S形速度曲线，被1,6-二磷酸果糖激活，并被二价铜离子抑制。在这些方面，它与从哺乳动物肝脏中分离出的酶相似。磷酸烯醇丙酮酸结合位点之间的相互作用程度取决于温度。
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引用本文的文献
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Biochem J. 1975 Mar;145(3):575-9. doi: 10.1042/bj1450575.
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