Esterases of Drosophila. II. Biochemical studies of esterase-5 in D. pseudoobscura.
In vitro enzyme hybridization was carried out with combinations of six allozymic variants of Esterase-5 from Drosophila pseudoobscura. Studies on heat stability and specific activity changes accompanying hybridization were done to examine the possible expression of overdominance at the biochemical level. In 11 of 15 combinations no significant change in specific activity was found following hybridization. In two cases hybridization resulted in a decrease in activity in the mixture, while in two cases esterase activity was elevated. Heat stability studies, in several cases, revealed reduced rates of inactivation in in vitro and in vivo heterozygotes compared with homozygotes. From these and other data a model for the molecular mechanism of heterosis is presented.
D000818:Animals; D003720:Densitometry; D004330:Drosophila / Q000201:enzymology*; D004586:Electrophoresis; D004950:Esterases / Q000032:analysis*; D005260:Female; D005799:Genes, Dominant; D008040:Genetic Linkage; D014644:Genetic Variation; D005838:Genotype; D006358:Hot Temperature; D006823:Hybrid Vigor; D006824:Hybridization, Genetic; D008297:Male; D008954:Models, Biological; D011110:Polymorphism, Genetic; D012730:Sex Chromosomes
D004950:Esterases