A comparative study of the enzymological features of .ALPHA.-amylase in the Drosophila melanogaster species subgroup.
- 1 January 1994
- journal article
- research article
- Published by Genetics Society of Japan in The Japanese Journal of Genetics
- Vol. 69 (3) , 251-258
- https://doi.org/10.1266/jjg.69.251
Abstract
A comparative study was done on the enzymological features of alpha-amylase among six sibling species belonging to the Drosophila melanogaster species subgroup. The pH optima were 7.6 for D. melanogaster, D. mauritiana and D. simulans and 7.4 for D. erecta, D. teissieri and D. yakuba. The temperature optima were commonly 37 C in all species studied. However, there are two types of temperature dependence; a strict one as observed in D. melanogaster, D. mauritiana and D. simulans, and a flat one as observed in D. erecta, D. teissieri and D. yakuba. These separations are consistent with the general phylogeny within this species subgroup. The substrate dependence was almost the same in all the species studied. The Vmax and Km were also estimated for each species. We found clear differences in the enzymological features between the species. Thus these differences might reflect an adaptation of the amylase enzyme system to speciation in this species subgroup.Keywords
This publication has 8 references indexed in Scilit:
- Evidence for adaptive evolution of the G6pd gene in the Drosophila melanogaster and Drosophila simulans lineages.Proceedings of the National Academy of Sciences, 1993
- Amino acid substitution at the Adh locus of Drosophila is facilitated by small population size.Proceedings of the National Academy of Sciences, 1993
- Adaptive protein evolution at the Adh locus in DrosophilaNature, 1991
- Adaptive significance of amylase polymorphism in Drosophila IV. A comparative study of biochemical properties of the alpha-amylase in DrosophilaMelanogaster, D. hydei, D. subobscura, and D. busckiiComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1989
- The functional significance of amylase polymorphism in Drosophila melanogaster I. Properties of two amylase variantsGenetica, 1978
- Protein Polymorphism as a Phase of Molecular EvolutionNature, 1971
- Amylase variants in Drosophila melanogaster: Linkage studies and characterization of enzyme extractsJournal of Experimental Zoology, 1969
- A PHOTOMETRIC METHOD FOR THE DETERMINATION OF α-AMYLASE IN BLOOD AND URINE, WITH USE OF THE STARCH-IODINE COLORJournal of Biological Chemistry, 1949