鳗鱼白肌丙酮酸激酶的纯化及动力学特性研究

The purification and kinetic characterization of eel white muscle pyruvate kinase.

作者信息

Roberts B, Anderson P J

出版信息

Comp Biochem Physiol B. 1985;80(1):51-6. doi: 10.1016/0305-0491(85)90421-3.

Abstract

A stable, homogeneous preparation of pyruvate kinase from white muscle of the American eel, Anguilla rostrata with a specific activity of 350 units/mg has been obtained. The enzyme has a pH optimum in the range 6.3-6.5 and requires Mg2+ and K+ for maximum activity. Eel muscle pyruvate kinase exhibits slight co-operativity in the binding of the substrate phosphoenol-pyruvate. It is activated by fructose-1,6-bisphosphate in a pH dependent manner and is inhibited by both alanine and phenylalanine. These properties are very similar to the properties of the mammalian M2 isozyme.

摘要

已从美洲鳗鲡（Anguilla rostrata）的白肌中获得了一种稳定、均匀的丙酮酸激酶制剂，其比活性为350单位/毫克。该酶的最适pH范围为6.3 - 6.5，最大活性需要Mg2+和K+。鳗鲡肌肉丙酮酸激酶在底物磷酸烯醇丙酮酸的结合中表现出轻微的协同性。它被1,6 - 二磷酸果糖以pH依赖的方式激活，并被丙氨酸和苯丙氨酸抑制。这些特性与哺乳动物M2同工酶的特性非常相似。