Skip to main content
Genetics logoLink to Genetics
. 1984 Mar;106(3):435–448. doi: 10.1093/genetics/106.3.435

Genetic Variation Affecting the Expression of Catalase in DROSOPHILA MELANOGASTER: Correlations with Rates of Enzyme Synthesis and Degradation

Glenn C Bewley 1, Cathy C Laurie-Ahlberg 1
PMCID: PMC1224248  PMID: 6423446

Abstract

Both second and third chromosome substitution lines isolated from natural populations of Drosophila melanogaster affect the expression of catalase (EC 1.11.1.6) at both the larval and adult stages of development. In each case, the level of catalase activity is strongly related to the level of catalase-specific cross-reacting material. Turnover studies employing the catalase inhibitor 3-amino-1,2,4-triazole were conducted on a selected number of lines. Although the variation in steady state levels of catalase protein was highly significant among lines, variation in intracellular degradation rate was not. These results suggest that the different steady state levels observed among lines largely reflect different rates of catalase synthesis.

Full Text

The Full Text of this article is available as a PDF (835.8 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Laurie-Ahlberg C. C., Maroni G., Bewley G. C., Lucchesi J. C., Weir B. S. Quantitative genetic variation of enzyme activities in natural populations of Drosophila melanogaster. Proc Natl Acad Sci U S A. 1980 Feb;77(2):1073–1077. doi: 10.1073/pnas.77.2.1073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Laurie-Ahlberg C. C., Williamson J. H., Cochrane B. J., Wilton A. N., Chasalow F. I. Autosomal factors with correlated effects on the activities of the glucose 6-phosphate and 6-phosphogluconate dehydrogenases in Drosophila melanogaster. Genetics. 1981 Sep;99(1):127–150. doi: 10.1093/genetics/99.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Laurie-Ahlberg C. C., Wilton A. N., Curtsinger J. W., Emigh T. H. Naturally occurring enzyme activity variation in Drosophila melanogaster. I. Sources of variation for 23 enzymes. Genetics. 1982 Oct;102(2):191–206. doi: 10.1093/genetics/102.2.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. PRICE V. E., STERLING W. R., TARANTOLA V. A., HARTLEY R. W., Jr, RECHCIGL M., Jr The kinetics of catalase synthesis and destruction in vivo. J Biol Chem. 1962 Nov;237:3468–3475. [PubMed] [Google Scholar]
  5. Woodbury W., Spencer A. K., Stahman M. A. An improved procedure using ferricyanide for detecting catalase isozymes. Anal Biochem. 1971 Nov;44(1):301–305. doi: 10.1016/0003-2697(71)90375-7. [DOI] [PubMed] [Google Scholar]

Articles from Genetics are provided here courtesy of Oxford University Press

RESOURCES