Abstract
The activity of purified deoxycytidylate deaminase obtained from chick-embryo extracts is dependent upon the presence of deoxycytidine triphosphate and magnesium ions. The stability of the enzyme at 37 degrees C is markedly enhanced by deoxycytidine triphosphate, and less so by the other deoxyribonucleotides. The inhibition by p-chloromercuribenzoate, urea, and deoxythymidine triphosphate, is reversed by deoxycytidine triphosphate. This reversal suggests that the regulation of enzyme activity is effected through configurational changes in the enzyme structure.
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