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 Amax at 276, 370 and 452 nm. The A452 and A370 decreased upon addition in anaerobiosis of spermine and spermidine or dithionite, but not putrescine. The enzyme had a Mr of ca 63 000 and a specific activity of 1200 nkat/mg at 37° with spermidine as substrate. It showed a Km for 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.
Purification and characterization of oat polyamine oxidase / R. Federico, C. Alisi, F. Forlani, R. Angelini. - In: PHYTOCHEMISTRY. - ISSN 0031-9422. - 28:8(1989), pp. 2045-2046.
Purification and characterization of oat polyamine oxidase
F. ForlaniPenultimo
;
1989
Abstract
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 Amax at 276, 370 and 452 nm. The A452 and A370 decreased upon addition in anaerobiosis of spermine and spermidine or dithionite, but not putrescine. The enzyme had a Mr of ca 63 000 and a specific activity of 1200 nkat/mg at 37° with spermidine as substrate. It showed a Km for 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.
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