Abstract
A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, 'antizyme inhibitor', was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a complex with antizyme. Therefore the antizyme inhibitor can be used to assay the amount of inactive ODC-antizyme complex formed in vitro. When assayed by this method, the complex was shown to be eluted before ODC from a Sephadex G-100 column. Significant increase in ODC activity was observed when the antizyme inhibitor was added to crude liver extracts from rats that had been injected with 1,3-diaminopropane to cause decay of ODC activity, suggesting the presence of inactive ODC-antizyme complex in the extracts.
MeSH Terms
Animals
Carboxy-Lyases/antagonists & inhibitors
Chromatography, Gel
Enzyme Activation/drug effects
Kinetics
Liver/metabolism
Male
Ornithine Decarboxylase Inhibitors
Proteins/antagonists & inhibitors
Rats
Rats, Inbred Strains
Chemicals
Ornithine Decarboxylase Inhibitors
Proteins
ornithine decarboxylase antizyme
Carboxy-Lyases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fujita K
Murakami Y
Hayashi S
References (19)
19 references, click to expand
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