Thermal Stability of Alpha-glycerophosphate Dehydrogenase in Drosophila
Overview
Overview
Authors
Authors
Affiliations
Affiliations
Soon will be listed here.
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.
References
1.
Ott L, Scandalios J
. Genetically defined peptidases of maize. I. Biochemical characterization of allelic and nonallelic forms. Biochem Genet. 1976; 14(7-8):619-34.
DOI: 10.1007/BF00485840.
View
2.
Macintyre R, OBrien S
. Interacting gene-enzyme systems in Drosophila. Annu Rev Genet. 1976; 10:281-318.
DOI: 10.1146/annurev.ge.10.120176.001433.
View
3.
Lakovaara S, Saura A, Lankinen P
. EVOLUTION AT THE α-GPDH LOCUS IN DROSOPHILIDAE. Evolution. 2017; 31(2):319-330.
DOI: 10.1111/j.1558-5646.1977.tb01014.x.
View
4.
Herrup K, Mullen R
. Biochemical and genetic factors in the heat inactivation of murine beta-glucuronidase. Biochem Genet. 1977; 15(7-8):641-53.
DOI: 10.1007/BF00484095.
View
5.
Li I, Daniel W
. Correlation between structural variation and activity of murine kidney beta-galactosidase: implications for genetic control. Biochem Genet. 1976; 14(11-12):933-52.
DOI: 10.1007/BF00485126.
View