Abstract
A particulate enzyme complex from Escherichia coli catalyzing the oxidation of lactate to pyruvate has been studied. Enzyme preparations obtained from celss of E. coli, grown in synthetic medium containing DL-lactate, oxidized both isomers of lactate. An acetone powder from such preparations oxidized D-lactateonly and required methylene blue for activity. Enzyme preparations from cells of E. coli, grown in media with glucose as the source of carbon, oxidized D-lactate vigorously but showed little or no oxidative activity in the presence of L-lactate. Some of the properties of the enyzme complex have been described and the relation of the findings to adaptive enzyme formation has ben discussed.
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