Aldehyde oxidase and xanthine dehydrogenase from wild-type Drosophila melanogaster and immunologically cross-reacting material from ma-1 mutants. Purification by immunoadsorption and characterization.

Abstract

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.