Polyamine oxidase from oat shoots was purified to homogeneity by the criteria of polyacrylamide gel electrophoresis in native and denaturing conditions. The purified yellow enzyme had an Amaxat 276, 370 and 452 nm. The A452and A370decreased upon addition in anaerobiosis of spermine and spermidine or dithionite, but not putrescine. The enzyme had a Mrof ca 63 000 and a specific activity of 1200 nkat/mg at 37° with spermidine as substrate. It showed a Kmfor spermine and spermidine of 6.0 μM and 9.5 μM respectively, the same pH optimum (6.8) for both substrates and was inhibited by N1-acetylspermine. © 1989.
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