Abstract
CDP reductase was separated from the cytosol of rat Yoshida ascites sarcoma. The precipitate, which resulted from the acidification of the cytosol by acetic acid at pH 5.2, catalyzed specifically the reduction of CDP, whereas the concurrently resulted supernatant catalyzed those of UDP, ADP and GDP. The CDP reductase showed a single peak in the pattern of the enzyme activity in DEAE-cellulose and also in Sepharose 4B column chromatography with adequate recovery of the activity.
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