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An amine oxidase in seedlings of Papaver somniferum L.

  • Published:
Biologia Plantarum

Abstract

Amine oxidase (AO) from 4-d-old seedlings of Papaver somniferum L. (Papaveraceae) was purified (58-fold) by using ammonium sulphate precipitation and chromatography on Sephadex G-150 and HA-Ultrogel columns. The most readily oxidized substrate was tyramine and other aromatic amines, while aliphatic amines cadaverine and putrescine were oxidized more slowly. Cu chelating and carbonyl reagents are the most effective inhibitors of poppy amine oxidase. Immunoblotting analysis showed cross reactivity of AO protein from poppy seedlings with polyclonal antisera against AO from pea. Obtained Mr value for AO from poppy (83 kDa) corresponds to that of copper AOs (75 – 90 kDa). These results suggest that the amine oxidase from poppy seedlings is a copper containing and tyramine specific AO.

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Abbreviations

AO:

amine oxidase

TO:

tyramine oxidase

PSAO:

amine oxidase of pea seedlings

DETC:

diethyldithiocarbamate

SDS:

sodium dodecyl sulphate

HA-Ultrogel:

microcrystalline hydroxyapatite

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Authors and Affiliations

  1. Department of Cell and Molecular Biology of Drugs, Faculty of Pharmacy, Comenius University, Kalinciakova 8, SK-83232, Bratislava, Slovak Republic

    A. Bilkova, L. Bezakova, F. Bilka & M. Psenak

Authors
  1. A. Bilkova
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  2. L. Bezakova
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  3. F. Bilka
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  4. M. Psenak
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Corresponding author

Correspondence to A. Bilkova.

Additional information

This work was supported by the grant of Slovak Grant Agency (VEGA 1/1197/04) and by the Comenius University, Faculty of Pharmacy Grant (FaF UK/1191/2002).

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Bilkova, A., Bezakova, L., Bilka, F. et al. An amine oxidase in seedlings of Papaver somniferum L.. Biol Plant 49, 389–394 (2005). https://doi.org/10.1007/s10535-005-0013-x

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  • DOI: https://doi.org/10.1007/s10535-005-0013-x

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