Molecular cloning of a cDNA coding for feline liver xanthine dehydrogenase

A cDNA coding for Feline liver xanthine dehydrogenase(XDH, EC1.1.1.204) was amplified by RT-PCR and cloned for determining the sequence:. The clones c ontained an open reading frame of 4002 base pairs encoding 1333 amino acid residues. The calculated molecular weight and isoelectric point were approx imately 146 kDa and 7.0. Comparison of the deduced amino acid sequences ind icated remarkable high homology, i.e., the amino acid residues of feline XD H shared approximately 90%, 87%, 87% and 86% identity with those of human, bovine, rat and mouse, respectively. The amino acid sequences of two putati ve iron-sulfur centers, one NAD binding site and one molybdenum binding sit e were well conserved among mammalian animals.