The purification and kinetic characterization of eel white muscle pyruvate kinase

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Abstract

1. 1. 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. 2. 2. The enzyme has a pH optimum in the range 6.3-6.5 and requires Mg2+ and K+ for maximum activity. 3. 3. Eel muscle pyruvate kinase exhibits slight co-operativity in the binding of the substrate phosphoenol-pyruvate. It is activated by fructose-1,6-biphosphate 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. © 1985.

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Roberts, B., & Anderson, P. J. (1985). The purification and kinetic characterization of eel white muscle pyruvate kinase. Comparative Biochemistry and Physiology -- Part B: Biochemistry And, 80(1), 51–56. https://doi.org/10.1016/0305-0491(85)90421-3

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