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Comparative Study
. 1981 Apr;19(3-4):311-20.
doi: 10.1007/BF00504276.

Thermal stability of alpha-glycerophosphate dehydrogenase in Drosophila

T Alatossava, S Lakovaara
Comparative Study

Thermal stability of alpha-glycerophosphate dehydrogenase in Drosophila

T Alatossava et al. Biochem Genet. 1981 Apr.

Abstract

Thermal stability of alpha-glycerophosphate dehydrogenase-1 (alpha-Gpdh-1) in nine Drosophila species was studied at pH's ranging form 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.

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