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Science 27 September 1963:
Vol. 141. no. 3587, pp. 1278 - 1279
DOI: 10.1126/science.141.3587.1278
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Articles

Feedback Control of Purified Deoxycytidylate Deaminase

Gladys F. Maley 1 and Frank Maley 1

1 Division of Laboratories and Research, New York State Department of Health, and Department of Biochemistry, Albany Medical College, Albany

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 °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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Science. ISSN 0036-8075 (print), 1095-9203 (online)