Polyamine oxidase from Zea mays shoots |
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Authors: | Yonezo Suzuki Eiji Hirasawa |
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Affiliation: | Laboratory of Plant Physiology, Biological Institute, University of Toyama, Gofuku, Toyama 930, Japan |
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Abstract: | Polyamine oxidase of maize shoots purified 10-fold had a pH optimum of 6·3 with spermidine as substrate, and Km of 6 × 10?4 M. The enzyme was inhibited by the acridine compounds quinacrine, 6,9-diamino-2-ethoxyacridine and acriflavin, but carbonyl reagents, typical thiol inhibitors and copper-binding agents were without effect. Inhibition by quinacrine was reversed by FMN and FAD. Furthermore, about 50 % of the activity of the apoenzyme was restored by the addition of FAD, but not by FMN or riboflavin, indicating that the maize polyamine oxidase is an FAD-dependent flavoprotein. |
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Keywords: | Gramineae maize spermidine spermine polyamine oxidase acridine compounds FAD. |
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