Abstract
Thermal stability of α-glycerophosphate dehydrogenase-1 (α-Gpdh-1) in nine Drosophila species was studied at pH's ranging from 6.4 to 8.5. This was done by measuring the changes in the activity of enzymes during the heat denaturation process. In addition to temperature, the rate of denaturation is highly dependent on the pH of the incubation buffer. The results of this study show that the thermal stability of enzyme molecules is different in different species. This holds true also in the species in which the enzymes have been found to be identical by other means. The differences between species of the Drosophila virilis group are discussed.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Alahiotis, S. (1979). Adaptation of Drosophila enzymes to temperature. I. Supernatant and mitochondrial malate dehydrogenase. Insect Biochem. 9189.
Alahiotis, S., Miller, S., and Berger, E. (1977). Natural selection at the α-GDH locus in Drosophila. Nature 269144.
Bewley, G. C., and Lucchesi, J. C. (1977). Origin of α-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster and their functional relationship in the α-glycerophosphate cycle. Biochem. Genet. 15235.
Bewley, G. C., Rawls, J. M., and Lucchesi, J. C. (1974). α-Glycerophosphate dehydrogenase in Drosophila melanogaster: kinetic differences and developmental differentation of the larval and adult isozymes. J. Insect Physiol. 20153.
Bienz, M., and Deak, I. I. (1978). Microelectrophoresis of α-glycerophosphate dehydrogenase isozymes in various tissues of wild-type and mutant Drosophila. Insect Biochem. 8449.
Collier, G. E. (1977). Inter- and intraspecific variation of α-glycerophosphate dehydrogenase among Drosophila. Isozyme Bull. 1058.
Collier, G. E., and MacIntyre, R. J. (1977). Microcomplement fixation studies on the evolution of α-glycerophosphate dehydrogenase within the genus Drosophila. Proc. Natl. Acad. Sci. USA 74684.
Coyne, J. A., Eanes, W. F., Ramshaw, J. A. M., and Koehn, R. (1979). Electrophoretic heterogeneity of α-glycerophosphate dehydrogenase among many species of Drosophila. Syst. Zool. 28164.
Hansford, R. G., and Sacktor, B. (1971). Oxidative metabolism of insecta. In Florkin, M., and Scheer, B. T. (eds.), Chemical Zoology Vol. 6, Academic, New York, pp. 213–247.
Herrup, K., and Mullen, R. J. (1977). Biochemical and genetic factors in the heat inactivation of murine β-glucuronidase. Biochem. Genet. 15641.
Komma, D. J. (1968). Glucose-6-phosphate dehydrogenase in Drosophila: sex-influenced electrophoretic variant. Biochem. Genet. 1229.
Lakovaara, S. (1969). Malt as a culture medium for Drosophila species. Drosoph. Inf. Serv. 44128.
Lakovaara, S., and Keränen, L. (1980). Variation at the α-Gpdh locus of drosophilids. Hereditas 92251.
Lakovaara, S., Saura, A., and Lankinen, P. (1977a). Evolution of the α-GPDH locus in Drosophilidae. Evolution 31319.
Lakovaara, S., Saura, A., and Lankinen, P. (1977b). Natural selection and the α-GPDH locus in Drosophilidae. In Christiansen, F. B., and Fenchel, T. M. (eds.), Measuring Selection in Natural Populations. Lecture Notes in Biomathematics Vol 19, Springer-Verlag, New York, pp. 245–264.
Li, I. C., and Daniel, W. L. (1976). Correlation between structural variation and activity of murine kidney β-galactosidase: implications for genetic control. Biochem. Genet. 14933.
MacIntyre, R. J., and O'Brien, S. J. (1976). Interacting gene-enzyme systems in Drosophila. Ann. Rev. Genet. 10281.
McDonald, J. F., and Avise, J. C. (1976). Evidence for the adaptive significance of enzyme activity levels: interspecific variation in α-GPDH and ADH in Drosophila. Biochem. Genet. 14347.
Miller, S., Pearcy, R. W., and Berger, E. (1975). Polymorphism at the α-glycerophosphate dehydrogenase locus in Drosophila melanogaster. I. Properties of adult allozymes. Biochem. Genet. 13175.
O'Brien, S. J., and MacIntyre, R. J. (1972a). The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7141.
O'Brien, S. J., and MacIntyre, R. J. (1972b). The α-glycerophosphate cycle in Drosophila melanogaster. II. Genetic aspects. Genetics 71127.
Ott, L. A., and Scandalios, J. G. (1976). Genetically defined peptidases of maize. I. Biochemical characterization of allelic and nonallelic forms. Biochem. Genet. 14619.
Sacktor, B. (1970). Regulation of intermediary metabolism with special reference to the control mechanisms in insect flight muscle. Adv. Insect Physiol. 7267.
Sacktor, B. (1975). Biochemistry of insect flight. In Candy, D. J., and Kilby, B. A. (eds.), Insect Biochemistry and Function Chapman and Hall, London, pp. 1–88.
Wright, D. A., and Shaw, C. R. (1969). Genetics and ontogeny of α-glycerophosphate dehydrogenase isozymes in Drosophila melanogaster. Biochem. Genet. 3343.
Author information
Authors and Affiliations
Additional information
This study was supported by funds from the National Research Council of Sciences of Finland.
Rights and permissions
About this article
Cite this article
Alatossava, T., Lakovaara, S. Thermal stability of α-glycerophosphate dehydrogenase in Drosophila . Biochem Genet 19, 311–320 (1981). https://doi.org/10.1007/BF00504276
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00504276