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. 1987 Dec;85(4):906–909. doi: 10.1104/pp.85.4.906

Polyamine Oxidase from Water Hyacinth

Purification and Properties

Hiroshi Yanagisawa 1, Akemi Kato 1, Sawa Hoshiai 1, Akiyoshi Kamiya 1, Naohiro Torii 1
PMCID: PMC1054367  PMID: 16665829

Abstract

Polyamine oxidase was purified to homogeneity from leaves of water hyacinth by the criterion of sodium dodecyl sulfate gel electrophoresis (SDS disc PAGE). The enzyme showed a high specificity for spermidine and spermine (Km values 28 micromolar and 20 micromolar, respectively). The optimal pH of the enzyme for both spermidine and spermine was 6.5. The molecular weight of the enzyme estimated by Sephadex G-200 gel filtration was 87,000, while SDS disc PAGE gave a single band at the molecular weight of 60,000. Octamethylenediamine and quinacrine were strong inhibitors of the enzyme, but p-chloromercuribenzoate was without effect. A prosthetic group in the enzyme was identified as flavin adenine dinucleotide.

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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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