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Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)

Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting pr...

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Published in:Journal of experimental botany 1999-01, Vol.50 (330), p.63-69
Main Authors: Omarov, Rustem T., Akaba, Shuichi, Koshiba, Tomokazu, Lips, S. Herman
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container_issue 330
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creator Omarov, Rustem T.
Akaba, Shuichi
Koshiba, Tomokazu
Lips, S. Herman
description Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting proteins were detected in barley plants capable of oxidizing a number of aliphatic and aromatic aldehydes such as indole-3-aldehyde, acetaldehyde, heptaldehyde, and benzaldehyde. Mouse polyclonal antibodies raised against purified maize AO cross-reacted with barley AO proteins extracted from roots, leaves and seeds. At least three different AO proteins were detected in roots on the basis of their mobility during PAGE after native Western blot analysis while in leaves and seeds only one polypeptide cross-reacted with the antibody. SDS-immunoblot analysis showed marked differences in molecular weight between subunits of the AO bands extracted from roots, leaves and seeds. Two distinct subunit bands were observed in roots, with relatively close molecular weights (160 kDa and 145 kDa), while a single subunit with a molecular weight of 150 kDa was observed in leaf and seed extracts. Menadione, a specific and potent inhibitor of animal AO did not affect barley AO proteins. Root and leaf AO differed in their thermostability and susceptibility to exogenous tungstate. The AO proteins in plants may be a group of enzymes with different substrate specificity, tissue distribution and presumably fulfilling different metabolic roles in each plant organ.
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Herman</creatorcontrib><title>Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)</title><title>Journal of experimental botany</title><addtitle>Journal of Experimental Botany</addtitle><description>Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting proteins were detected in barley plants capable of oxidizing a number of aliphatic and aromatic aldehydes such as indole-3-aldehyde, acetaldehyde, heptaldehyde, and benzaldehyde. Mouse polyclonal antibodies raised against purified maize AO cross-reacted with barley AO proteins extracted from roots, leaves and seeds. 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source Oxford Journals Online; JSTOR Archival Journals
subjects Aldehyde oxidase
Aldehydes
Barley
Biological and medical sciences
Cell and Molecular Biology, Biochemistry and Molecular Physiology
Enzymes
Fundamental and applied biological sciences. Psychology
Leaves
Metabolism
molybdenum cofactor (MoCo)
Nitrates
Oxidases
Plant physiology
Plant physiology and development
Plant roots
Plants
roots
Seedlings
seeds
Tungstates
title Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)
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