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Among three AO isoforms detected in pea plants, the activity of PAO-1 was dominant in leaves of seedlings and young leaves of mature plants, while PAO-3 revealed the highest band intensity in old leaves and roots. PAO-1 and PAO-3 are homodimers consisting of 145 kDa and 140 kDa subunits, respectively, while PAO-2 is a heterodimer of one 145 kDa and one 140 kDa subunit. In leaves, the activity of PAO-1 disappeared gradually with leaf ageing, while in roots it was present only in seedlings but not in mature pea plants. PAO-3 could oxidize abscisic aldehyde, a precursor of abscisic acid, indicating the possible involvement of this isoform in ABA synthesis in pea. The ability of PAO-3 to oxidize abscisic aldehyde was higher in old leaves than in young ones and increased significantly both in roots and leaves of plants exposed to salinity and ammonium treatments. A marked increase of the AO protein level was observed after ammonium application but not under salinity. Interestingly, the activity of PAO isoforms may be transcriptionally and post-transcriptionally regulated during vegetative growth and in response to stress conditions, and such a regulation might be particularly important to adjust ABA levels to the recent requirements of the plant. The observations suggest that the AO isoforms have different metabolic roles and that the activity and protein level of each isoform is regulated not only by environmental conditions but also through plant developmental stages.

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Aldehyde oxidase (AO; EC 1.2.3.1) isoforms in roots of barley plants grown on ammonium or nitrate as nitrogen sources were studied. Roots of ammonium-grown barley plants exhibited considerable levels of AO2, AO3, and AO4 activities after native PAGE. Significantly lower AO2 and AO3 activity bands were observed in roots of plants grown on nitrate. When abscisic aldehyde was used as a substrate a strong response of the AO2 band was observed as well as a faint reaction of the AO3 band, but no activity of AO4 was observed using this substrate. The 160 and 145 kDa polypeptides were detected in ammonium grown plants. Root extracts of nitrate-fed plants revealed only a minor 145 kDa protein band and none of the 160 kDa subunit was detected. The assembly of the AO3 heterodimer requires the simultaneous presence of 160 and 145 kDa subunits. Subunit analysis of AO2 and AO4 revealed homodimeric composition of 160 and 145 kDa, respectively. Western blot analysis revealed changing AO subunits levels during germination and plant development. Differential expression of AO subunits (160 and 145 kDa) and subsequent formation of isoforms, which differ in substrate specificity, distribution and fulfil different enzymatic reactions, may constitute an important regulatory mechanism in the plant.