Alcohol dehydrogenase thermostability variants in Drosophila melanogaster: comparison of activity ratios and enzyme levels.

Representatives of five allozymic classes of Drosophila alcohol dehydrogenase have been compared with respect to their activity levels on two alcohol substrates, quantities of ADH protein, and stability in crude extracts. Within each allozymic class, strains from widely diverse geographic locations differ in their enzyme activity levels but are identical for a measure known as "activity ratio," which is obtained by dividing the average activity reading on isopropanol by that obtained with ethanol. They are also similar in the rate at which ADH activity declines in crude extracts held at 25 degrees C. For several of the fast-resistant and fast-moderate strains, differences in ADH activity are associated with differences in the amount of enzyme present. The catalytic efficiencies of the fast-resistant forms are considerably lower than those of the fast-moderate allozymes. The origin and persistence of the rare but ubiquitous fast-resistant allozyme is discussed.