Abstract
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.
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