Purification and characterization of oat polyamine oxidase

  • Federico R
  • Alisi C
  • Forlani F
 et al. 
  • 4

    Readers

    Mendeley users who have this article in their library.
  • 17

    Citations

    Citations of this article.

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 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.

Author-supplied keywords

  • Avena sativa
  • Gramineae
  • oat
  • polyamine oxidase.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free