Purification and properties of ornithine decarboxylase from rat liver.
Ornithine decarboxylase was purified to homogeneity, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and polyacrylamide gel electrofocusing, about 710,000-fold with a 35% yield from the liver cytosol of thioacetamide-treated rats. The final specific activity was approximately 24,400 nmol/min/mg of protein. The apparent molecular weight of the enzyme determined by gel filtration analyses on Sephacryl S-200 was 55,000 in the presence of 0.25 M NaCl and 145,000 in its absence. The minimum molecular weight of the enzyme was determined to be 54,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was estimated as 5.7 in the presence of 8 M urea. Some catalytic properties of the enzyme were also studied.
D000818:Animals; D002262:Carboxy-Lyases / Q000302:isolation & purification*; D003600:Cytosol / Q000201:enzymology; D005260:Female; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D009955:Ornithine Decarboxylase / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013853:Thioacetamide / Q000494:pharmacology
D046911:Macromolecular Substances; D013853:Thioacetamide; D002262:Carboxy-Lyases; D009955:Ornithine Decarboxylase