Production of Homo- and Hetero-Dimeric Isozymes from Two Aldehyde Oxidase Genes of Arabidopsis thaliana

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Abstract
Polyclonal antibodies were raised against synthetic peptides or recombinant polypeptides encoded by Arabidopsis atAO-1 and atAO-2 cDNAs, which have sequences similar to maize and animal aldehyde oxidase (AO) cDNAs. Anti-atAO-1 antibodies recognized AOa and A0β among the three isoforms, AOα, AOβ, and AOγ, detected in Arabidopsis seedlings after native PAGE, while anti-atAO-2 antibodies reacted with AOβ and AOγ. The polypep-tide specifically recognized by each antibody was collected as the Protein-A/IgG/antigen complex. The 150- and 146-kDa polypeptides were purified by SDS-PAGE and digested with Achromobacter Protease I. From the amino acid sequences and molecular masses of the derivative peptides, it was revealed that the 150- and 145-kDa polypeptides were the products of atAO-1 and atAO-2, respectively. Molecular masses of the native forms of AOα, AOβ, and AOγ were estimated as approximately 290–300 kDa. These results suggest that AOα and AOγare homodimers consisting of atAO-1 and atAO-2 products, respectively, and that AOβ is a heterodimer of the atAO-1 and atAO-2 products.

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