biologia plantarum

International journal on Plant Life established by Bohumil Němec in 1959

Biologia plantarum 49:389-394, 2005 | DOI: 10.1007/s10535-005-0013-x

An amine oxidase in seedlings of Papaver somniferum L.

A. Bilková1,*, L. Bezáková1, F. Bilka1, M. Pšenák1
1 Department of Cell and Molecular Biology of Drugs, Faculty of Pharmacy, Comenius University, Bratislava, Slovak Republic

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.

Keywords: aromatic amines; cadaverine; Cu-amine oxidase; immunoblotting; poppy; putrescine
Subjects: amine oxidase; cadaverine; morphine biosynthesis; opium poppy, aromatic amines; Papaver somniferum; pea, amine oxidase; Pisum sativum; poppy, aromatic amines; putrescin; sanguinarine biosynthesis; tyramine oxidase

Received: March 22, 2004; Accepted: February 11, 2005; Published: September 1, 2005  Show citation

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Bilková, A., Bezáková, L., Bilka, F., & Pšenák, M. (2005). An amine oxidase in seedlings of Papaver somniferum L. Biologia plantarum, 49(3), 389-394. doi: 10.1007/s10535-005-0013-x
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