ABSTRACT
Polyamine oxidases that act at the secondary amino group would be further subdivided according to whether diaminopropane or aminopropionaldehyde were among the products. The highest specific activity was found in the peroxisomal fraction, where its presence has been confirmed histochemically in both rat liver and kidney, although polyamine oxidase was not included in a recent review of peroxisomal oxidases. The level of polyamine oxidase activity in samples of bovine milk, from animals in full lactation, was found to be remarkably constant. Inhibition by aminoguanidine and 3-hydroxybenzyloxyamine was similar in both bovine serum and milk. The cytotoxic or cytostatic effects of oxidized polyamines in vitro have been well documented for a wide variety of cell types including bacteria, trypanosomes, mammalian spermatozoa, bacterial, plant, and animal viruses, tumor cells, and a number of mammalian cell lines. Although some of the observed cytotoxicity of oxidized polyamines may be attributable to the formation of acrolein in long-term incubations.
