Abstract
The mode of degradation of adenosine by extracts of Aspergillus terricola was suggested to be affected preliminary by adenosine deaminase to inosine and the resulting ribonucleoside was then degraded hydrolytically to give hypoxanthine and ribose. With regard to guanosine, the same extracts could initially catalyze the hydrolytic cleavage of guanosine to guanine and ribose. The resulting base was then deaminated to give xanthine by guanine deaminase. Addition of arsenate to the reaction mixture or dialyzing the extract did not affect the observed hydrolytic activity indicating the absence of phosphorylase activity or phosphorylase-phosphatase activities in the extracts.
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