BIOCHEMICAL GENETICS OF PURINE CATABOLISM IN DROSOPHILA MELANOGASTER
- 1 January 1964
- journal article
- research article
- Published by Genetics Society of Japan in The Japanese Journal of Genetics
- Vol. 39 (4) , 222-239
- https://doi.org/10.1266/jjg.39.222
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.Keywords
This publication has 12 references indexed in Scilit:
- STUDIES ON THE MUTANT MAROON-LIKE IN DROSOPHILA MELANOGASTERGenetics, 1960
- MUTANTS OF DROSOPHILA MELANOGASTER DEFICIENT IN XANTHINE DEHYDROGENASEGenetics, 1959
- COMPARATIVE STUDIES OF VARIOUS INHIBITORS ON XANTHINE OXIDASE AND RELATED ENZYMESJournal of Biological Chemistry, 1955
- STUDIES ON METALLOFLAVOPROTEINS .1. XANTHINE OXIDASE, A MOLYBDOFLAVOPROTEIN1954
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Properties of Mutants of Drosophila Melanogaster and Changes During Development as Revealed by Paper ChromatographyProceedings of the National Academy of Sciences, 1951
- THE L-AMINO ACID OXIDASES OF SNAKE VENOM .2. ISOLATION AND CHARACTERIZATION OF HOMOGENEOUS L-AMINO ACID OXIDASE1950
- PTERINE OXIDASE1949
- DIFFERENTIAL SPECTROPHOTOMETRY OF PURINE COMPOUNDS BY MEANS OF SPECIFIC ENZYMES .1. DETERMINATION OF HYDROXYPURINE COMPOUNDS1947
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934