Di Matteo G, Di Prisco G, Romeo G
Biochim Biophys Acta. 1976 May 13;429(3):694-704. doi: 10.1016/0005-2744(76)90318-1.
Nuclear glutamate dehydrogenase (EC 1.4.1.3) activity has been demonstrated in Chinese hamster ovary cells. Some characteristics of this enzyme have been examined and compared with those of the mitochondrial glutamate dehydrogenase from the same source. Differences were detected in the extent of the activation by inorganic phosphate, in the pH versus activity curves, in the affinity of the two enzymes for the cofactor NAD+ and in the electrophosretic mobility. A different rate of decay of the two enzymes has been observed in cells grown in the presence of chloramphenicol. Immunological studies show that, as in ox liver, the nuclear enzyme has specific antigenic determinants besides those in common with mitochondrial glutamate dehydrogenase. Finally, experiments of thermal inactivation indicate a higher stability of the mitochondrial enzyme.
已在中国仓鼠卵巢细胞中证实了核谷氨酸脱氢酶(EC 1.4.1.3)的活性。已对该酶的一些特性进行了检测,并与来自同一来源的线粒体谷氨酸脱氢酶的特性进行了比较。在无机磷酸盐的激活程度、pH与活性曲线、两种酶对辅因子NAD+的亲和力以及电泳迁移率方面检测到了差异。在氯霉素存在下生长的细胞中观察到了两种酶不同的衰减速率。免疫学研究表明,与牛肝中的情况一样,除了与线粒体谷氨酸脱氢酶共有的抗原决定簇外,核酶还有特定的抗原决定簇。最后,热失活实验表明线粒体酶具有更高的稳定性。