Polyamine Oxidase from Water Hyacinth
Author(s) -
Hiroshi Yanagisawa,
Akemi Kato,
Sawa Hoshiai,
Akiyoshi Kamiya,
Naohiro Torii
Publication year - 1987
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.85.4.906
Subject(s) - spermidine , polyamine oxidase , spermine , sephadex , chemistry , polyamine , flavin group , enzyme , biochemistry , putrescine , sodium dodecyl sulfate , size exclusion chromatography , gel electrophoresis , flavoprotein , polyacrylamide gel electrophoresis , chromatography
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 (K(m) 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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