Abstract
Sucrose (and a variety of glycols) caused inhibition of the glutamate specific catalytic activity of glutamate dehydrogenase and stimulation of the monocarboxylic acid activity. In addition, sucrose prevented the concentration dependent aggregation of the enzyme and produced a sharp increase in stability toward heat denaturation. These studies suggest the potential usefulness of sucrose in studying protein structure transitions, but demand caution in the use of such media for separation and characterization of macromolecules unless possible effects on structure are taken into account.
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