Functional significance of amylase polymorphism in Drosophila melanogaster. III. Ontogeny of amylase and some alpha-glucosidases.
Changes in amylase (E.C. 3.2.1.1), maltase (E.C. 3.2.1.20), sucrase, and PNPGase activities in relation to changes in wet weight and protein content were studied during the development of larvae and adult flies from two strains of Drosophila melanogaster, homozygous for different amylase alleles. All alpha-glucosidase activities increase exponentially during a large part of larval development, parallel to the increase in weight, and drop at the end of the third instar. Amylase activity of the Amy1 strain follows the same pattern. In contrast, amylase activity of the Amy4,6 strain continues its exponential increase longer. In the third larval instar amylase activity in the Amy4,6 strain becomes much higher than in the Amy1 strain. During the first hours of adult life amylase activity of the two strains does not differ. Then Amy4,6 activity starts to rise and becomes much higher (4-5 times) than Amy1 amylase activity, which remains approximately constant. All adult enzyme activities are much higher than in larvae. Comparison of enzyme activity of amylase and alpha-glucosidases in larvae and adults confirms that differences in amylase activities can become important only when starch is a limiting factor in the food.
D000681:Amylases / Q000235:genetics*; D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics / Q000254:growth & development*; D005959:Glucosidases / Q000235:genetics*; D007814:Larva / Q000201:enzymology; D008675:Metamorphosis, Biological; D011110:Polymorphism, Genetic; D000520:alpha-Glucosidases / Q000235:genetics*
D000681:Amylases; D005959:Glucosidases; D000520:alpha-Glucosidases