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 is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Abraham, I., and Doane, W. W. (1976). Temporal gene controlling midgut amylase activity patterns in Drosophila melanogaster. Genetics 83:s1.
Bakker, K. (1959). Feeding period, growth and pupation in larvae of Drosophila melanogaster. Entomol. Exp. Appl. 2171.
Bakker, K. (1961). An analysis of factors which determine success in competition for food among larvae of Drosophila melanogaster. Arch. Neerl. Zool. 14200.
Bodenstein, D. (1950). The postembryonic development of Drosophila. In Demerec, M. (ed.), Biology of Drosophila Wiley, New York.
Chovnick, A., Gelbart, W., McCarron, M., Osmond, B., Candido, E. P. M., and Baillie, D. L. (1976). Organization of the rosy locus in Drosophila melanogaster: Evidence for a control element adjacent to the xanthine dehydrogenase structural element. Genetics 84233.
Cohen, P. T. W., Omenn, G. S., Motulsky, A. G., Chen, S. H., and Giblett, E. R. (1973). Restricted variation in the glycolytic enzymes of human brain and erythrocytes. Nature 241229.
Day, T. H., and Needham, L. (1974). Properties of alcohol dehydrogenase isozymes in a strain of Drosophila melanogaster homozygous for the Adh-slow allele. Biochem. Genet. 11167.
Day, T. H., Hillier, P. C., and Clarke B. (1974a). Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochem. Genet. 11141.
Day, T. H., Hillier, P. C., and Clarke, B. (1974b). The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster. Biochem. Genet. 11155.
De Jong, G., and Scharloo, W. (1976). Environmental determination of selective significance or neutrality of amylase variation in Drosophila melanogaster. Genetics 8477.
De Jong, G., Hoorn, A. J. W., Thörig, G. E. W., and Scharloo, W. (1972). Frequencies of amylase variants in Drosophila melanogaster. Nature 238453.
Dickinson, W. J. (1971). Aldehyde oxidase in Drosophila melanogaster: A system for genetic studies on developmental regulation. Dev. Biol. 2677.
Doane, W. W. (1969a). Amylase variants in Drosophila melanogaster: Linkage studies and characterization of enzyme extracts. J. Exp. Zool. 171321.
Doane, W. W. (1969b). Drosophila amylases and problems in cellular differentiation. In Hanly, R. W. (ed.), RNA in Development University of Utah Press; Salt Lake City.
Doane, W. W. (1977). Further evidence for temporal genes controlling Amy expression in Drosophila melanogaster. Genetics 86:s15.
Fox, D. J. (1971). The soluable citric acid cycle enzymes of Drosophila melanogaster. I. Genetics and ontogeny of NADP-linked isocitrate dehydrogenase. Biochem. Genet. 569.
French, D. (1975). Chemistry and biochemistry of starch. In Whelan, W. J. (ed.), Biochemistry, Ser. 1, Vol. 5: Biochemistry of Carbohydrates.
Gillespie, J. H., and Kojima, K. (1968). The degree of polymorphism in enzymes involved in energy production compared to that in nonspecific enzymes in two Drosophila ananassae populations. Proc. Natl. Acad. Sci. 61528.
Hassett, C. C. (1948). The utilization of sugars and other substances by Drosophila. Biol. Bull. 95114.
Hoorn, A. J. W., and Scharloo, W. (1978a). The functional significance of amylase polymorphism in Drosophila melanogaster. I. Properties of two amylase variants. Genetica 49173.
Hoorn, A. J. W., and Scharloo, W. (1978b). The functional significance of amylase polymorphism in Drosophila melanogaster. II. Properties and distribution of some α-glucosidases. Neth. J. Zool. 291.
Johnson, G. B. (1974). Enzyme polymorphism and metabolism. Science 18428.
Kikkawa, H. (1964). An electrophoretic study on amylase in Drosophila melanogaster. Jap. J. Genet. 39401.
Kühner, J., and Hansen, K. (1975). Chromatographic isolation of α-glucosidases from the taste hair rich tarsi of the fly Protophormia terraenovae: Their possible role as sugar receptor proteins. J. Comp. Physiol. 99257.
Lewontin, R. C. (1974). The Genetic Basis of Evolutionary Change Columbia University Press, New York.
Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193265.
Noelting, G., and Bernfild, P. (1948). Sur les enzymes amylolytiques. III. La β-amylase: Dosage d'activité et contrôle du l'absence d'α-amylase. Helv. Chim. Acta 31286.
O'Brien, S. J., and MacIntyre, R. J. (1972). The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7141.
Powell, J.R. (1975). Protein variation in natural populations of animals. Evol. Biol. 879.
Puijk, K., and De Jong, G. (1972). α-Amylases in a population of Drosophila melanogaster from Dahomey. Drosophila Inform. Serv. 4961.
Rechsteiner, M. (1970). Drosophila lactate dehydrogenase and α-glycerophosphate dehydrogenase: Distribution and change in activity during development. J. Insect Physiol. 16957–977.
Robertson, F. W. (1963). The ecological genetics of growth in Drosophila b: Correlation between the duration of the larval period and bodysize in relation to larval diet. Gernet. Res. 474.
Sang, J. H. (1956). The quantitative nutritional requirements of Drosophila melanogaster. J. Exp. Biol. 3345.
Sonnenblick, B. (1950). The embryology of Drosophila. In Demerec, M. (ed.), The Biology of Drosophila Wiley, New York.
Strasburger, M. (1932). Bau, Funktion und Variabilität des Darmtraktus von Drosophila melanogaster Meigen. Z. Wiss. Zool. 140539.
Thompson, J. N., Ashburner, M., and Woodruff, R. C. (1977). Presumptive control mutation for alcohol dehydrogenase in Drosophila melanogaster. Nature 270263.
Warburg, O., and Christian, W. (1941). Isolierung und Kristallisation des Gärungsferments Enolase. Biochem. Z. 310384.
Ward, R. D. (1975). Alcohol dehydrogenase activity in Drosophila melanogaster: A quantitative character. Genet. Res. 2681.
Author information
Authors and Affiliations
Additional information
The investigations were supported by the Foundation for Fundamental Biological Research (BION), which is subsidized by the Netherlands Organization for the Advancement of Pure Research (Z.W.O.).
Rights and permissions
About this article
Cite this article
Hoorn, A.J.W., Scharloo, W. Functional significance of amylase polymorphism in Drosophila melanogaster. III. Ontogeny of amylase and some α-glucosidases. Biochem Genet 18, 51–63 (1980). https://doi.org/10.1007/BF00504359
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00504359