Purification, cDNA Cloning, and Tissue Distribution of Bovine Liver Aldehyde Oxidase

Marco Li-Calzi, Carlo Raviolo, Elena Ghibaudi, Luca De Gioia, Mario Salmona, Giovanni Cazzaniga, Mami Kurosaki, Mineko Terao, Enrico Garattini
1995 Journal of Biological Chemistry  
Aldehyde oxidase was purified to homogeneity from bovine liver and primary structural information obtained by sequencing a series of cleavage peptides permitted the cloning of the corresponding cDNA. The cDNA is 4,630 base pairs long, and it consists of a 102base pair 5-untranslated region followed by a 4017-base pair coding region and a 511-base pair 3-untranslated region. The open reading frame predicts a 1339-amino acid polypeptide with a calculated molecular weight of 147,441, which is
more » ... stent with the size of the aldehyde oxidase monomeric subunit. The aldehyde oxidase polypeptide contains consensus sequences for iron-sulfur centers and a molybdopterin binding site. The amino acid sequence deduced from the cDNA shows significant similarity with that of xanthine dehydrogenases from various sources. The primary structure of bovine aldehyde oxidase is remarkably similar (approximately 86%) to that of the translation product of a cDNA recently isolated by Wright et al. (Wright, R. M., Vaitaitis, G. M., Wilson, C. M., Repine, T. B., Terada, L. S., and Repine, J. E. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 10690 -10694 ) and reported to represent human xanthine dehydrogenase. With the help of a monospecific antibody raised against the purified protein and the isolated cDNA, the tissue distribution of the bovine aldehyde oxidase protein and corresponding mRNA was determined. Aldehyde oxidase is expressed at high levels in liver, lung, and spleen, and, at a much lower level, in many other organs. Aldehyde oxidase (aldehyde-oxygen oxidoreductase; EC 1.2.3.1; AO) 1 catalyzes the oxidation of endogenous and exogenous N-heterocyclic compounds in the presence of O 2 (1). The enzyme belongs to the family of molybdenum-containing pro-
doi:10.1074/jbc.270.52.31037 pmid:8537361 fatcat:sapluwk3jbbhpjg5zdudxaqu4i