Functional significance of amylase polymorphism in Drosophila melanogaster. III. Ontogeny of amylase and some ?-glucosidases
- 1 February 1980
- journal article
- research article
- Published by Springer Nature in Biochemical Genetics
- Vol. 18 (1-2) , 51-63
- https://doi.org/10.1007/bf00504359
Abstract
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 α-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 Amy 1 strain follows the same pattern. In contrast, amylase activity of the Amy 4,6 strain continues its exponential increase longer. In the third larval instar amylase activity in the Amy 4,6 strain becomes much higher than in the Amy 1 strain. During the first hours of adult life amylase activity of the two strains does not differ. Then Amy 4,6 activity starts to rise and becomes much higher (4–5 times) than Amy 1 amylase activity, which remains approximately constant. All adult enzyme activities are much higher than in larvae. Comparison of enzyme activity of amylase and α-glucosidases in larvae and adults confirms that differences in amylase activities can become important only when starch is a limiting factor in the food.This publication has 35 references indexed in Scilit:
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