Heat Denaturation of Bovine Liver Glutamate Dehydrogenase
Heat Denaturation of Bovine Liver Glutamate Dehydrogenase
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牛肝谷氨酸脱氢酶的热变性
DOI：
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发表时间：
1975
期刊：
影响因子：
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通讯作者：
K. S. Rogers
中科院分区：
文献类型：
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作者：
K. S. Rogers
牛肝谷氨酸脱氢酶在47 ℃下发生热变性，酶活性丧失，形成无活性的不溶性蛋白质。分数损失的催化活性与蛋白质荧光和相应百分比的蛋白质分子的溶解度的改变相一致。在操作上，在50%变性时，酶分子总群体的一半是完全催化活性和可溶性的，而蛋白质分子群体的另一半是完全无催化活性和不溶的。感谢K博士。E. Guyer，E. S.克莱恩湖D. Abbott和E. S. Higgins提供有用的建议。
Summary Heat denaturation of bovine liver glutamate dehydrogenase occurred at 47° with loss of enzyme activity and formation of inactive, insoluble protein. Fractional loss of catalytic activity coincided with alteration in protein fluorescence and solubility for a corresponding percentage of protein molecules. Operationally, at 50% denaturation, one-half of the total population of enzyme molecules is fully active catalytically and soluble and the other half of the protein molecule population is completely inactive catalytically and insoluble. The author thanks Drs. K. E. Guyer, E. S. Kline, L. D. Abbott, and E. S. Higgins for helpful suggestions.