Irreversible inhibition of nuclear exoribonuclease by thymidine-3'-fluorophosphate and p-haloacetamidophenyl nucleotides.
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.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002467:Cell Nucleus / Q000201:enzymology*; D006219:Halogens / Q000494:pharmacology*; D006367:HeLa Cells / Q000201:enzymology*; D007461:Iodoacetates / Q000494:pharmacology; D009711:Nucleotides / Q000494:pharmacology*; D012316:RNA Nucleotidyltransferases / Q000037:antagonists & inhibitors; D012260:Ribonucleases / Q000037:antagonists & inhibitors*
D006219:Halogens; D007461:Iodoacetates; D009711:Nucleotides; D012316:RNA Nucleotidyltransferases; D012260:Ribonucleases