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Regulation of enzyme activities in Drosophila: II. Characterization of enzyme responses in aneuploid flies

Published online by Cambridge University Press:  14 April 2009

John M. Rawls Jr  and
John C. Lucchesi
John M. Rawls Jr
Affiliation:
Department of Zoology and Curriculum in Genetics, University of North Carolina, Chapel Hill, North Carolina 27514, U.S.A.
John C. Lucchesi
Affiliation:
Department of Zoology and Curriculum in Genetics, University of North Carolina, Chapel Hill, North Carolina 27514, U.S.A.

Summary

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To test whether large changes in the enzyme levels of segmentally aneuploid Drosophila melanogaster can be ascribed to changes in kinetic properties of the enzymes affected, comparisons have been made with regard to the heat stability, substrate concentration dependency, and the presence of heat-stable inhibitors or activators within the extracts of aneuploid and control flies. By these criteria, no differences were found between controls and the α-GPDH activity of flies trisomic for chromosome II segments 27D–31E, 35A–40, 41–45F, and 57B–60F and no differences were evident between the IDH properties of 70CD–71B aneuploids and their controls. The enzyme changes observed in these aneuploids are more likely associated with changes in the rates of accumulation of the enzyme molecules. The IDH of flies trisomic for the 27D–31E region was more heat-stable than that of controls while the α-GPDH of flies trisomic for the 21A–25CD region displayed an apparent Michaelis constant for α-glycerophosphate lower than that of controls. The possible bases for these latter qualitative distinctions are discussed.

Type
Research Article
Information
Genetics Research , Volume 24 , Issue 1 , August 1974 , pp. 73 - 80
Copyright
Copyright © Cambridge University Press 1974

References

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