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Plant and Cell Physiology, 1980, Vol. 21, No. 6 1085-1094
© 1980

Article

Purification and properties of maize polyamine oxidase: a flavoprotein

Yonezo Suzuki and Hiroshi Yanagisawa

Department of Biology, Faculty of Science, Osaka City University Sumiyoshi-ku, Osaka 558, Japan

Polyamine oxidase was purified from maize shoots to homogeneity by the criteria of polyacrylamide gel electrophoresis and ultracentrifugation. The purified yellow enzyme showed absorption maxima at 278, 380 and 460 nm. The molecular weight estimated by gel filtration was about 65,000 and the sedimentation coefficient was 5.95 S. Sodium dodecylsulfate gel electrophoresis yielded a single band at a molecular weight of 65,000. The enzyme contained 1 mole of FAD per mole of enzyme. Amino acid composition and kinetic properties of the enzyme are presented.

(Received April 30, 1980; )
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