Wild-type Drosophila melanogaster exhibit increased levels of xanthine dehydrogenase when grown on synthetic semi-defined media. The increased activity is accompanied by an altered mobility of the enzyme's electrophoretic on polyacrylamide gels, but not by an increase in cross-reacting material to antibody against xanthine dehydrogenase, or by a significant alteration in the K m for 2-amino-4-hydroxypteridine. These data indicate that an activation of enzyme occurs, possibly by a co-factor involved in the activity. This hypothesis is supported by the lack of increase in cross-reacting materials and by a lack of increase in xanthine dehydrogenase activity in lxd flies raised on synthetic media, since lxd is thought to be defective in the formation of the possible co-factor. In the flies raised on synthetic media, the increased levels of xanthine dehydrogenase activity are reflected principally in the fat-body and lymph enzyme. The activities of pyridoxal oxidase and aldehyde oxidase, enzymes related to xanthine dehydrogenase, are also increased in flies raised on the synthetic media, but kynurenine formamidase, an enzyme not related to xanthine dehydrogenase, is not increased.
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