Abstract
Ornithine decarboxylase ( l-ornithine carboxy-lyase, EC 4.1.1.17) was purified about 5400-fold from the soluble fraction of liver from thioacetamide-treated rats. The purified enzyme showed only a single protein band on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be approx. 100 000. Its isoelectric point was found to be at pH 4.1 and its optimal pH around 7.0. The K m value for l-ornithine was 2·10 −4 M at pH 7.0. The enzyme required thiol compounds for maximal activity and was inhibited by inhibitors of pyridoxal enzymes, such as l-canaline and isonicotinic acid hydrazide. Among the various amino acids and amines tested, putrescine and d-ornithine caused a weak inhibition, while other compounds had little effect. The properties of ornithine decarboxylase from the liver of thioacetamide-treated rats were compared with those of enzyme from regenerating rat liver.
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