PURIFICATION AND PROPERTIES OF RAT-BRAIN GLUTAMATE-DEHYDROGENASE
PURIFICATION AND PROPERTIES OF RAT-BRAIN GLUTAMATE-DEHYDROGENASE
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DOI：
10.1111/j.1471-4159.1979.tb11705.x
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发表时间：
1979-01-01
影响因子：
4.7
通讯作者：
FAHIEN, LA
中科院分区：
文献类型：
--
作者：
CHEE, PY;DAHL, JL;FAHIEN, LA
描述了一种从大鼠大脑中制备高纯度谷氨酸脱氢酶的方法。当该酶在十二烷基硫酸钠（SDS） - 聚丙烯酰胺凝胶上进行电泳时，仅检测到1条蛋白质条带。就SDS - 聚丙烯酰胺凝胶电泳、免疫化学特性和大多数动力学参数而言，大鼠大脑中的酶与大鼠肝脏中的酶基本相同。大脑中的酶与谷氨酸的反应性低得多，对氟哌啶醇的抑制更敏感，并且比肝脏中的酶稳定得多。
A method is described for the preparation of glutamate dehydrogenase in a highly purified form from rat brain. Only 1 protein band was detected when the enzyme was subjected to electrophoresis on SDS [sodium dodecyl sulfate] polyacrylamide gels. The rat brain enzyme was essentially identical to the rat liver enzyme with respect to electrophoresis on SDS polyacrylamide gels, immunochemical properties and most kinetic parameters. The brain enzyme was much less reactive with glutamate, was more sensitive to inhibition by haloperidol, and was considerably more stable than the liver enzyme.