title: [Genotypical peculiarities of expression of the beta-specific carboxylic ester hydrolase allozymes in Drosophila melanogaster of wild type].
abstract: Using the method of computer densitometry we have determined the expression level of the electrophoretically separated S- and F-allozymes of beta-specific esterase (E.C. 3.1.1.2) in Drosophila melanogaster homozygotes and heterozygotes for beta-Est locus. alpha-naphtylacetate, beta-naphtylacetate and alpha-naphtylpropionate were used as substrates. Expression intensity of the esterases was estimated using the quantity of the reaction product which is created as a result of simultaneous azocoupling between naphtol and diazonium during 4, 24, 44 and 64 min of incubation time. We have established the reliable differences between the Sand F-allozyme expression depending on the beta-Est locus structure. In all the variants the higher level of summary activity S- and F-allozymes of beta-esterase of the heterozygotes comparing to those of two types of homozygotes was demonstrated independently of the Drosophila sex. We compared the characteristics of the expression dynamics of the allozymes of dominant homozygotes (beta-Est(S)/beta-Est(S)), heterozygotes (beta-Est(S) beta-Est(F)) and recessive homozygotes (beta-Est(F)/beta-Est(F)). We also consider some possible mechanisms of heterosis of S- and F-allozyme expression according to the theory of biochemical enrichment of heterozygote genotypes.
authors.forename: A M
authors.initials: AM
authors.lastname: Andrievskiĭ
mesh_terms: D000483:Alleles; D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000235:genetics*; D029721:Drosophila Proteins / Q000235:genetics*; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005838:Genotype; D006579:Heterozygote; D006720:Homozygote; D007527:Isoenzymes / Q000235:genetics; D008297:Male; D013379:Substrate Specificity
chemical_list: D029721:Drosophila Proteins; D007527:Isoenzymes; D002265:Carboxylic Ester Hydrolases