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From the
1 From the Department of Molecular Biology and the Virus Laboratory, University of California, Berkeley, California 94720
Aspartate transcarbamylase, a regulatory enzyme from Escherichia coli, has been prepared by a procedure which yields approximately 5 g of highly purified enzyme from 700 g of wet packed bacterial cells. Purified aspartate transcarbamylase was dissociated by treatment with p-hydroxymercuribenzoate to yield two kinds of protein subunits which were separated by column chromatography. The separated subunits retained their functional properties, namely, catalytic activity or affinity for the regulatory metabolite, cytidine triphosphate.
The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits
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