Aldehyde oxidase and xanthine dehydrogenase from wild-type Drosophila melanogaster and immunologically cross-reacting material from ma-1 mutants. Purification by immunoadsorption and characterization.
The pleiotropic effect of the ma-1 mutation on the enzymes xanthine dehydrogenase and aldehyde oxidase in Drosophila melanogaster can most readily be explained by assuming that the enzymes share a subunit or cofactor whose synthesis is controlled by the ma-1 locus. According to this hypothesis a protein or a tightly bound cofactor common to both enzymes should be inactive or missing in the corresponding immunologically cross-reacting material found in ma-1 flies. Three of the proteins involved were purified by immunoadsorption: xanthine dehydrogenase, xanthine dehydrogenase cross-reacting material and aldehyde oxidase.
D000445:Aldehyde Oxidoreductases / Q000276:immunology / Q000302:isolation & purification; D000818:Animals; D001665:Binding Sites; D003429:Cross Reactions; D004331:Drosophila melanogaster / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis; D005779:Immunodiffusion; D007454:Iodides / Q000494:pharmacology; D007501:Iron / Q000032:analysis; D007658:Ketone Oxidoreductases / Q000276:immunology; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D008970:Molecular Weight; D008982:Molybdenum / Q000032:analysis; D009154:Mutation; D011485:Protein Binding; D014968:Xanthine Dehydrogenase / Q000276:immunology / Q000302:isolation & purification
D007454:Iodides; D046911:Macromolecular Substances; D005182:Flavin-Adenine Dinucleotide; D008982:Molybdenum; D007501:Iron; D014968:Xanthine Dehydrogenase; D000445:Aldehyde Oxidoreductases; D007658:Ketone Oxidoreductases