Rogers K S
Proc Soc Exp Biol Med. 1975 Sep;149(4):1023-5. doi: 10.3181/00379727-149-38948.
Heat denaturation of bovine liver glutamate dehydrogenase occurred at 47 degrees 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.
牛肝谷氨酸脱氢酶的热变性发生在47摄氏度,伴随着酶活性丧失以及无活性、不溶性蛋白质的形成。催化活性的部分丧失与相应比例蛋白质分子的蛋白质荧光和溶解度变化相一致。从操作上来说,在50%变性时,酶分子总数的一半具有完全的催化活性且可溶,而另一半蛋白质分子群体在催化方面完全无活性且不溶。