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.
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Suzuki et al. (1980) studied this question.