来自欧洲鲈肝脏的6-磷酸葡萄糖酸脱氢酶的纯化及性质

Purification and properties of the enzyme 6-phosphogluconate dehydrogenase from Dicentrarchus labrax L. liver.

作者信息

del Mar Medina-Puerta M, Garrido-Pertierra A

出版信息

Comp Biochem Physiol B. 1986;83(1):215-20. doi: 10.1016/0305-0491(86)90355-x.

Abstract

The enzyme 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP+ oxidoreductase, decarboxylating EC 1.1.1.44) from bass liver has been purified to over 95% of homogeneity by gel filtration, affinity and ion exchange chromatographies. The apparent molecular weight was estimated by gel filtration chromatography to about 100,000. Analysis of the enzyme on sodium dodecyl sulphate polyacrylamide gel electrophoresis showed to be a dimeric protein. The effect of pH and kinetic properties were studied.

摘要

通过凝胶过滤、亲和色谱和离子交换色谱法，已将鲈鱼肝脏中的6-磷酸葡萄糖酸脱氢酶（6-磷酸-D-葡萄糖酸：NADP +氧化还原酶，脱羧酶，EC 1.1.1.44）纯化至纯度超过95％。通过凝胶过滤色谱法估计其表观分子量约为100,000。在十二烷基硫酸钠聚丙烯酰胺凝胶电泳上对该酶进行分析，结果表明它是一种二聚体蛋白质。研究了pH值的影响和动力学性质。