泽蛙红细胞丙酮酸激酶的纯化、催化及调节特性

Purification, catalytic and regulatory properties of Rana ridibunda erythrocyte pyruvate kinase.

作者信息

Kaloyianni-Dimitriades M G, Beis I D

出版信息

Comp Biochem Physiol B. 1984;79(2):245-50. doi: 10.1016/0305-0491(84)90021-x.

Abstract

Pyruvate kinase of Rana ridibunda erythrocytes is one of the regulatory enzymes of glycolysis. PK was purified about 7800-fold. The purified enzyme showed on SDS-electrophoresis three protein bands with an apparent molecular weight of between 60 and 65 kD. The enzyme is subject to activation by FDP and to inhibition by ATP. It showed Km values for PEP and ADP of 0.095 and 0.98 mM respectively. It was activated by K+, Mg2+ and Ca2+ ions whereas it was inhibited by Na+ ions. The role of PK of Rana ridibunda erythrocytes, as a key and rate controlling enzyme of the glycolytic flux is discussed.

摘要

泽蛙红细胞丙酮酸激酶是糖酵解的调节酶之一。丙酮酸激酶被纯化了约7800倍。纯化后的酶在SDS电泳上显示出三条蛋白带，表观分子量在60至65kD之间。该酶受到1,6-二磷酸果糖（FDP）的激活和ATP的抑制。它对磷酸烯醇式丙酮酸（PEP）和二磷酸腺苷（ADP）的米氏常数（Km）分别为0.095和0.98 mM。它被钾离子（K+）、镁离子（Mg2+）和钙离子（Ca2+）激活，而被钠离子（Na+）抑制。本文讨论了泽蛙红细胞丙酮酸激酶作为糖酵解通量的关键和速率控制酶的作用。