STUDIES OF TREHALASE AND SUCRASE OF DROSOPHILA MELANOGASTER

Drosophila melanogaster possesses trehalase and sucrase activities that have a similar pH optima and heat labilities but are completely distinct forms as revealed by clear differences in electrophoretic mobility, pH inactivation, and their near-complete separation by ion-exchange chromatography. Both enzymes show a similar developmental pattern that includes a rapid, parallel increase in specific activity at the pupal-adult transition. Trehalase and sucrase are both partitioned between a membrane-bound and a free, soluble state although the enzymes in these two states appear to be similar in the several properties examined. Sucrase is not present as a single form, but consists of a family of isoenzymes that are separable into discrete fractions, but which are similar to each other by several criteria. © 1969.