Oxidation of spermine by an amine oxidase from lentil seedlings.

نویسندگان

  • A Cogoni
  • A Padiglia
  • R Medda
  • P Segni
  • G Floris
چکیده

Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in TI-HCI buffer; the K(m) value is 4.4.10(-4) molar, similar to that found with other substrates (putrescine and spermidine).

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عنوان ژورنال:
  • Plant physiology

دوره 95 2  شماره 

صفحات  -

تاریخ انتشار 1991