[Genotypical peculiarities of expression of the beta-specific carboxylic ester hydrolase allozymes in Drosophila melanogaster of wild type].

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.

[Genetic structure of the experimental population of Drosophila melanogaster polymorphic with respect to beta-carboxyesterase locus].

The polymorphism of beta-phile carboxyesterase (E.C.3.1.1.2) in the males and females of the wild type (Odessa 1) experimental population of Drosophila melanogaster Meigen has been studied with the polyacrylamide disc-electrophoresis. Two isoforms of the enzyme and three phenotypic classes non-uniformly presented among the males and females have been detected. The frequencies of the alleles encoding the corresponding isoforms of the beta-phile carboxyesterase have been determined, as well as those of the genotypes that differed qualitatively and quantitatively with respect to the investigated gene-enzyme system. The deviations of the detected genotype frequencies from the theoretically expected ones were determined. The role of the natural selection directed towards the decreasing of the frequencies of the certain allele is discussed.

[Expressivity of the gene-enzymatic system and viability indicators in the ontogenesis of Drosophila inbred lines and hybrids]. / Ekspressivnost' gen-énzimnykh sistem i pokazateli zhiznesposobnosti v ontogeneze inbrednykh linii i gibridov drozofily.

The activity, physico-chemical properties and multiple molecular forms of enzymes (alcohol dehydrogenase, superoxide dismutase, nonspecific alpha- and beta-esterases, hydroxide peptidohydrolase) were studied in ontogenesis of Drosophila inbred lines and their hybrids under conditions of high temperature (37-41 degrees C) and the presence in food of 10% ethanol. It was established that resistance of individuals to the effect of high temperature and alcohol, including manifestation of adaptive heterosis in hybrids not always depends on the level of the activity of enzymes analysed and is rather determined by allelic state of the appropriate structural genes. So, in conditions of the alcohol stress the individuals containing highly active F form of alcohol dehydrogenase have selective advantage and flie with hybrid F/S enzyme of higher activity and heat stability are more stable to the effect of high temperature. It is supposed that the complexes of adaptation genes (CGA) are formed in individuals of populations in response to the regular action of unfavourable environmental factors. These complexes condition optimal allelic control and most efficient regulation of enzyme activity in environment. Genotypic adaptation of individuals as well as occurrence of adaptive heterosis in hybrids seem likely to be connected with formation of CGA.

[A method of isolation of partially purified alkaline peptide hydrolase from Drosophila melanogaster larvae]. / Metod polucheniia chastichno ochishchennoi shchelochnoi peptidgidrolazy iz lichinok Drosophila melanogaster.

A semipreparative method is developed for preparing peptidohydrolase from Drosophila melanogaster larvae which involves the stages of extraction, salting-out, gel-filtration and ion-exchange chromatography. It is established that the maximal (up to 81%) yield of the enzyme is observed with the single extraction in the alkaline medium. The main bulk of the enzyme is salted-out in the low acid 3 M ammonium sulphate solution. Gel-filtration on column with Sephadex-25 provides complete salting-out of the enzyme-containing fraction, and ion exchange chromatography on CM-cellulose--a considerable purification of the enzyme under study. A degree of the obtained purification of the enzyme under study. A degree of the obtained peptidohydrolase preparation purity in acid and alkaline medium is determined by the method of electrophoresis in PAAG. At all stages of the preparation the enzyme possesses the casein-lytic activity and is able of hydrolyzing the ethyl ester and benzoyl arginine p-nitroanilide.

[Mutagenic effect of a tetrahydrodiazopyrene derivative on bacteria]. / O mutagennom deistvii proizvodnogo tetragidrodiazopirena na bakterii.

Mutagenic action of 3,7-diamino-4,9-dioxy-5,10-dioxo-4,5,9,10-tetrahydro-4,9-diazapiren (DDDTDP) was shown using indicator strains Salmonella typhimurium TA 1534, TA 1536, TA 1537, TA 1538. The drug-induced mutations in strains TA 1534 and TA 1538, and it can be used as a positive control in testing mutagens capable of inducing frameshift mutations. No significant differences was observed between DDDTDP effects on strains TA 1534 and TA 1538 which did or did not bear rfa mutation causing defects of cell wall lypopolysacharide complex. Within the range of concentrations tested DDDTDP had mutagenic effect without causing essential killing of bacteria. The mutagenic effect was decreased in the in vitro system of metabolic activation (Ames' plate test in Salmonella microsomes).