Irreversible Inhibition of Nuclear Exoribonuclease by Thymidine-3′-Fluorophosphate and p -Haloacetamidophenyl Nucleotides
- 20 June 1969
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 164 (3886), 1408-1410
- https://doi.org/10.1126/science.164.3886.1408
Abstract
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.Keywords
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