Journal of Experimental Botany, Vol 50, 63-69, Copyright © 1999 by Oxford University Press
R Omarov, S Akaba, T Koshiba and S Lips
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.Keywords: Aldehyde oxidase, barley, roots,
leaves, seeds, molybdenum cofactor (MoCo).
ARTICLES
Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)
Biostress Research Laboratory (J. Blaustein Institute for Desert Researches) and Department of Life Sciences (Faculty of Natural Sciences), Ben-Gurion University of the Negev, Sede Boqer 84990, Israel; Department of Biology, Tokyo Metropolitan University, Hachioji-shi, Tokyo 192-0397, Japan; Corresponding author; Fax: +972 7 6596752; E-mail: omarov@bgumail.bgu.ac.il
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