Irreversible Inhibition of Nuclear Exoribonuclease by Thymidine-3'-Fluorophosphate and p-Haloacetamidophenyl Nucleotides

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Science  20 Jun 1969:
Vol. 164, Issue 3886, pp. 1408-1410
DOI: 10.1126/science.164.3886.1408


Exoribonuclease purified from Ehrlich ascites tumor cell nuclei and in intact HeLa cell nuclei is irreversibly inactivated by tow concentrations of p-bromo- and p-iodoacetamidophenyl nucleotides and by thymidine-3'-fluorophosphate. Iodoacetate, bromoacetate, and thymidine-5'-fluorophosphate do not affect the enzyme. Although p-haloacetamidophenyl nucleotides inactivate ribonucleic acid polymerase of isolated HeLa cell nuclei, thymidine-3'-fluorophosphate does not affect the activity of this enzyme in vitro.

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