Skip to main content
SpringerLink
Log in

Regulation of amylase activity in Drosophila melanogaster: Variation in the number of enzyme molecules produced by different amylase genotypes

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Purified amylases from high- and low-activity variants of Drosophila melanogaster showed identical specific activities. Immunoelectrophoresis of crude larval homogenates showed severalfold differences between strains in the amounts of cross-reacting material. Control of amylase activity is “trans”-acting in heterozygotes between high- and low-activity variants. These results suggest the existence of polymorphic regulatory genes affecting the production levels of amylase protein in D. melanogaster.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Abraham, I., and Doane, W. W. (1978). Genetic regulation of tissue-specific expression of Amylase structural genes in Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 754446.

    Google Scholar 

  • Bahn, E. (1967). Crossing over in the chromosomal region determining amylase isozymes in Drosophila melanogaster. Hereditas 581.

    Google Scholar 

  • Bernfeld, P. (1955). Amylases. In Colowick, S., and Kaplan, N. (eds.), Methods in Enzymology Academic Press, New York, pp. 149–158.

    Google Scholar 

  • DeJong, G., Hoorn, A. J. W., Thorig, G. W. E., and Scharloo, W. (1972). Frequencies of amylase variants in Drosophila melanogaster. Nature 238453.

    Google Scholar 

  • Doane, W. W. (1969). Amylase variants in Drosophila melanogaster: Linkage studies and characterization of enzyme extracts. J. Exp. Zool. 171321.

    Google Scholar 

  • Doane, W. W. (1970). Drosophila amylases and problems in cellular differentiation. In Hanly, E. W. (ed.), RNA in Development (Int. Symp. Prob. Biol. 1, 1996), University of Utah Press, Salt Lake City, pp. 73–109.

    Google Scholar 

  • Doane, W. W. (1980). Midgut amylase activity patterns in Drosophila: Nomenclature. Dros. Inform. Serv. 5536.

    Google Scholar 

  • Doane, W. W., Abraham, I., Kolar, M. M., Martenson, R. E., and Deibler, G. E. (1975). Purified Drosophila α-amylase isozymes: Genetical, biochemical and molecular characterization. In Markert, C. L. (ed.), Isozymes, Vol. IV Academic Press, New York, pp. 585–607.

    Google Scholar 

  • Hickey, D. A. (1977). Selection for amylase allozymes in Drosophila melanogaster. Evolution 31800.

    Google Scholar 

  • Hickey, D. A. (1979). Selection on amylase allozymes in Drosophila melanogaster: Selection experiments using several independently derived pairs of chromosomes. Evolution 331128.

    Google Scholar 

  • Hoorn, A. J. W., and Scharloo, W. (1978a). The functional significance of amylase polymorphism in Drosophila melanogaster. 1. Properties of two amylase variants. Genetica 49173.

    Google Scholar 

  • Hoorn, A. J. W., and Scharloo, W. (1978b). The functional significance of amylase polymorphism in Drosophila melanogaster. V. The effect of food components on amylase and α-glucosidase activity. Genetica 49181.

    Google Scholar 

  • Laurell, C.-B. (1966). Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal. Biochem. 1545.

    Google Scholar 

  • Lewis, N., and Gibson, J. (1978). Variation in amount of enzyme protein in natural populations. Biochem. Genet. 16159.

    Google Scholar 

  • Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193265.

    Google Scholar 

  • McCarron, M., O'Donnell, J., Chovnick, A., Bhullar, B. S., Hewitt, J., and Candido, E. P. M. (1979). Organization of the rosy locus in Drosophila melanogaster: Further evidence in support of a cis-acting control element adjacent to the xanthine dehydrogenase structural element. Genetics 91275.

    Google Scholar 

  • McDonald, J. F., and Ayala, F. J. (1978). Genetic and biochemical basis of enzyme activity variation in natural populations. 1. Alcohol dehydrogenase in Drosophila melanogaster. Genetics 89371.

    Google Scholar 

  • Nielsen, J. T. (1977). Variation in the number of genes coding for salivary amylase in the bank vole, Clethrionomys glareola. Genetics 85155.

    Google Scholar 

  • Ouchterlony, O. (1958). Diffusion-in-gel methods for immunological analysis. Process Allergy 51.

    Google Scholar 

  • Prakash, S., Lewontin, R. C., and Hubby, J. L. (1969). A molecular approach to the study of genic heterozygosity in natural populations. IV. Patterns of genic variation in central, marginal and isolated populations of D. pseudoobscura. Genetics 61841.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biological Sciences, Brock University, L2S 3A1, St. Catharines, Ontario, Canada

    D. A. Hickey

Authors
  1. D. A. Hickey
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

This work was supported by Grant GM-21279 from the Institute of General Medical Science of the NIH to R. C. Lewontin and by an Operating Grant from the Natural Sciences and Engineering Research Council Canada to D. A. Hickey.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hickey, D.A. Regulation of amylase activity in Drosophila melanogaster: Variation in the number of enzyme molecules produced by different amylase genotypes. Biochem Genet 19, 783–796 (1981). https://doi.org/10.1007/BF00484009

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484009

Key words

Search

Navigation