SUMMARY: Spermine oxidized by partially purified serum amine oxidase inhibited the growth of a variety of Gram-positive and Gram-negative bacteria. This inhibition of growth was not antagonized by calcium ion, and occurred over a wide pH range. Inactivation increased with time and temperature of incubation. The antibacterial action was abolished by treating oxidized spermine with sodium borohydride. Oxidized spermine inhibited protein synthesis as shown by incorporation of C-valine into cellular protein and by inhibition of β-galactosidase induction. Incorporation of C-uracil into the nucleic acids of was not inhibited by oxidized spermine.


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