Effects of detergent on ornithine decarboxylase from rat liver. Stabilization and renaturation.
Ornithine decarboxylase was purified approximately 37000-fold with a 15% yield from livers of rats pretreated with thioacetamide. The specific activity of the final preparation, 1039 units/mg protein, was about four-times higher than the highest yet reported for the rat liver enzyme. The partially purified enzyme was quite labile but the labile enzyme was dramatically stabilized by the presence of either ethylene glycol or Tween 80. The detergent appeared to serve not only stabilization of the enzyme but also renaturation of the denatured enzyme.
D000818:Animals; D002262:Carboxy-Lyases / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008099:Liver / Q000201:enzymology*; D009955:Ornithine Decarboxylase / Q000302:isolation & purification*; D011489:Protein Denaturation / Q000187:drug effects; D051381:Rats; D011919:Rats, Inbred Strains; D012967:Sodium Dodecyl Sulfate; D012995:Solubility; D013501:Surface-Active Agents
D003902:Detergents; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate; D002262:Carboxy-Lyases; D009955:Ornithine Decarboxylase