来自鲈鱼（欧洲鲈鱼）肝脏的NADP依赖型异柠檬酸脱氢酶。
NADP-dependent isocitrate dehydrogenase from bass (Dicentrarchus labrax L.) liver.
作者信息
Medina-Puerta M M, Gallego-Iniesta M, Garrido-Pertierra A
机构信息
Departamento de Bioquímica, Facultad de Veterinaria, Universidad Complutense de Madrid, Spain.
出版信息
Biochem Int. 1988 Sep;17(3):489-98.
The isocitrate dehydrogenase from bass liver was purified to homogeneity by gel filtration, affinity and ion exchange chromatographies. The molecular weight was estimated by gel filtration chromatography to about 120,000. Analysis of the enzyme on sodium dodecyl sulphate polyacrylamide gel electrophoresis showed it to be a dimeric protein. The enzyme showed maximum activity in the pH range between 7.0 and 8.0 while its maximum activity was at pH 7.5. DL-Isocitrate and Mn2+ stabilized the enzyme, while NADP had the opposite effect. The Km for isocitrate was 0.31 mM and the Km for NADP was 36 microM.
通过凝胶过滤、亲和色谱和离子交换色谱法，将鲈鱼肝脏中的异柠檬酸脱氢酶纯化至同质。通过凝胶过滤色谱法估计其分子量约为120,000。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。该酶在pH 7.0至8.0范围内表现出最大活性，其最大活性在pH 7.5时出现。DL-异柠檬酸和Mn2+可使该酶稳定，而NADP则具有相反的作用。异柠檬酸的Km值为0.31 mM，NADP的Km值为36 microM。
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