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. 1982 Jun 15;204(3):647–652. doi: 10.1042/bj2040647

A macromolecular inhibitor of the antizyme to ornithine decarboxylase.

K Fujita, Y Murakami, S Hayashi
PMCID: PMC1158403  PMID: 7126159

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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