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°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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Publication Info
- Year
- 1963
- Type
- article
- Volume
- 141
- Issue
- 3587
- Pages
- 1278-1279
- Citations
- 14
- Access
- Closed
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Identifiers
- DOI
- 10.1126/science.141.3587.1278