Abstract
Biochemical properties of esterase 6 in Drosophila melanogaster were investigated using partially purified preparations from three genotypes, 1/1, 1/2, and 2/2. The molecular weight of the enzyme is estimated to be about 90,000, and treatment with sodium dodecylsulfate cleaves the enzyme into four units with a molecular weight of about 22,000. The activity toward 28 naturally occurring esters was assayed and shown to vary considerably with substrate, the 1/1 preparation having in general higher activity than 1/2 and 2/2, which were very similar. Heat sensitivity, the effect of metal ions, and the effects of the presence or absence of an end product were also studied. The differences demonstrated between allozymes would allow considerable scope, under appropriate conditions, for differential selection to operate between genotypes.
Similar content being viewed by others
References
Band, H. T. (1975). A survey of isozyme polymorphism in a Drosophila melanogaster natural population. Genetics 80761.
Barker, D. L., and Jencks, W. P. (1969). Pig liver esterase: Physical properties. Biochemistry 83879.
Beardmore, J. A. (1973). Genetic studies of polymorphic esterases in Drosophila. Atti. Accad. Sci. Inst. Bologna Ann. Mem. Ser. III 26153.
Beckman, L., and Johnson, F. M. (1964). Esterase variations in Drosophila melanogaster. Hereditas 51212.
Beckman, L., and Nilson, L. R. (1965). Variation of serum enzymes in bird species and hybrids. Hereditas 53221.
Birley, A. J., and Beardmore, J. A. (1972). Manifold large selective effects in an enzyme polymorphism. 5th Mar. Biol. Symp., Piccin. Edit., Padova, pp. 81–100.
Birley, A. J., and Beardmore, J. A. (1977). Genetical composition, temperature, density and selection in an enzyme polymorphism. Heredity 39133.
Burch, J. (1954). The purification and properties of horse liver esterase. Biochem. J. 58415.
Christiansen, F. B., Frydenberg, O., Glydenholm, A. O., and Simonsen, V. (1974). Genetics of Zoarces populations. VI. Further evidence, based on age group samples, of a heterozygote deficit in the Est III polymorphism. Hereditas 77225.
Danford, N. D., and Beardmore, J. A. (1978). Effects of insecticides in vitro and in vivo on esterase-6 in Drosophila melanogaster. Comp. Biochem. Physiol. 61C47.
Davis, B. J. (1964). Disc electrophoresis. II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121404.
de Jong, G., and Scharloo, W. (1976). Environmental determination of selective significance or neutrality of amylase variants in Drosophila melanogaster. Genetics 8477.
Frieden, C. (1971). Protein-protein interaction and enzymatic activity. Ann. Rev. Biochem. 40653.
Gibson, J. (1970). Enzyme flexibility in Drosophila melanogaster. Nature 227959.
Harris, H. (1971). Polymorphism and protein evolution. J. Med. Genet. 8444.
Inger, R. F., Voris, H. K., and Voris, H. H. (1974). Genetic variation and population ecology of some south-east Asian frogs of the genera Bufo and Rana. Biochem. Genet. 12121.
Jacobson, K. B., Murphy, J. B., and Hartman, F. C. (1970). Isoenzymes of Drosophila alcohol dehydrogenase. I. Isolation and interconversion of different forms. J. Biol. Chem. 2451075.
Kaziro, Y., Ochoa, S., Warner, R. C., and Chen, J. (1961). Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase. J. Biol. Chem. 2361917.
Koehn, R. K. (1969). Esterase heterogeneity: Dynamics of a polymorphism. Science 163943.
Kojima, K., and Yarbrough, K. M. (1967). Frequency-dependent selection at the esterase-6 locus in Drosophila melanogaster. Proc. Natl. Acad. Sci. 57645.
Lewontin, R. C. (1974). The Genetic Basis of Evolutionary Change, Columbia University Press, London.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reaction. J. Biol. Chem. 193265.
MacIntyre, R. J., and Wright, T. R. F. (1966). Response of esterase-6 alleles of Drosophila melanogaster and D. simulans to selection in experimental populations. Genetics 53371.
Manwell, C., and Kerst, K. V. (1966). Possibilities of biochemical taxonomy of bats using hemoglobin, lactate dehydrogenase, esterases and other proteins. Comp. Biochem. Physiol. 17741.
McDonald, J. F., and Avise, J. C. (1976). Evidence for the adaptive significance of enzyme activity levels: Interspecific variation in α-GDPH and ADH in Drosophila. Biochem. Genet. 14347.
Mittler, S., and Bennett, J. (1962). A simple food medium that requires no live yeast with the minimum of variables. Drosophila Inform. Serv. 41201.
Nachlas, M. M., and Seligman, A. M. (1949). Evidence for the specificity of esterase and lipase by the use of three chromogenic substrates. J. Biol. Chem. 181343.
Nevo, E. (1978). Genetic variation in natural populations: Patterns and theory. Theor. Popul. Biol. 13121.
Ornstein, L. (1964). Disc electrophoresis. I. Background and theory. Ann. N.Y. Acad. Sci. 121321.
Roderick, T. H., Ruddle, F. H., Chapman, V. M., and Shows, T. B. (1971). Biochemical polymorphisms in field and inbred mice (Mus musculus). Biochem. Genet. 5457.
Shapiro, A. L., Viñuela, E., and Maizel, J. V. (1967). Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28815.
Shaw, C. R., and Prasad, R. (1970). Starch gel electrophoresis of enzymes—A compilation of recipes. Biochem. Genet. 4297.
Smith, I. (1968). Chromatographic and Electrophoretic Techniques, Vol. 2: Zone Electrophoresis, Heinemann, London.
Ward, R. D. (1974). Alcohol dehydrogenase in Drosophila melanogaster: Activity variation in natural populations. Biochem. Genet. 12449.
Wright, T. R. F. (1963). The genetics of an esterase in Drosophila melanogaster. Genetics 48787.
Author information
Authors and Affiliations
Additional information
Supported in part by an SRC Research Studentship (N.D.D.).
Rights and permissions
About this article
Cite this article
Danford, N.D., Beardmore, J.A. Biochemical properties of esterase 6 in Drosophila melanogaster . Biochem Genet 17, 1–22 (1979). https://doi.org/10.1007/BF00484470
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00484470