Abstract
An eye color mutant of Drosophila melanogaster, ry, contained no uric acid at any developmental stage, but accumulated a large amount of hypoxanthine as compared with the amount of xanthine at pupal and imaginal stages. The xanthine dehydrogenase was revealed as an enzyme concerned with uric acid production in D. melanogaster of the wild type. It was suggested that xanthine dehydrogenase produced in the ry mutant was an enzyme molecule lacking the active site of xanthine oxidation. The activity of guanase, which catalyzes the conversion of guanine to xanthine, was observed in pupal and imaginal stages of both wild and ry strains. Thus it was shown that xanthine, which is a precursor of uric acid, was derived not only from hypoxanthine with dehydrogenase but also from guanine with guanase.
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