A comparative study of enzyme activity variation between ?-glycerophosphate and alcoholdehydrogenases in Drosophila melanogaster

Genetica ◽  
1981 ◽  
Vol 55 (1) ◽  
pp. 75-79 ◽  
Author(s):  
Patricia G. Wilson ◽  
John F. McDonald
Keyword(s):  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Comparative Study ◽  
Activity Variation ◽  
Enzyme Activity Variation

scholarly journals Causes and consequences of esterase 6 enzyme activity variation in pre-adult Drosophila melanogaster

Heredity ◽  
1994 ◽  
Vol 73 (2) ◽  
pp. 160-169 ◽  
Author(s):  
John G Oakeshott ◽  
Marlene Saad ◽  
Anne Y Game ◽  
Marion J Healy
Keyword(s):  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Activity Variation ◽  
Esterase 6 ◽  
Enzyme Activity Variation ◽  
Adult Drosophila

Genetic and environmental effects on the expression of peptidases and larval viability in Drosophila melanogaster.

Genetics ◽  
1992 ◽  
Vol 131 (3) ◽  
pp. 625-642 ◽  
Author(s):  
K Hiraizumi ◽  
P A Tavormina ◽  
K D Mathes
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Osmotic Stress ◽  
Genetic Background ◽  
Aminopeptidase Activity ◽  
Osmotic Concentration ◽  
Isogenic Lines ◽  
Activity Variation ◽  
Enzyme Activity Variation

Abstract The peptidase system in Drosophila melanogaster, consisting of dipeptidase-A, dipeptidase-B, dipeptidase-C and the leucine aminopeptidases, was used as a model to study the adaptive significance of enzyme activity variation. The involvement of the peptidases in osmoregulation has been suggested from the ubiquitous distribution of peptidase activities in nearly all tissues and the high concentration of amino acids and oligopeptides in the hemolymph. Under this hypothesis, larvae counteract increases in environmental osmotic stress by hydrolyzing peptides into amino acids both intra- and extracellularly to increase physiological osmotic concentration. The expression of the peptidases was studied by assaying for peptidase activities in third instar larvae of isogenic lines, which were reared under increasing levels of environmental osmotic stress using either D-mannitol or NaCl. Second and third chromosome substitution isogenic lines were used to assess the relative contribution of regulatory and structural genes in enzyme activity variation. Results indicate that: (1) genetic variation exists for peptidase activities, (2) the effect of osmotic stress is highly variable among peptidases, (3) changes in peptidase activities in response to osmotic stress depend on both genetic background and osmotic effector and (4) peptidase activities are correlated with each other, but these phenotypic correlations depend on genetic background, osmotic effector, and level of osmotic stress. Osmotic concentration in the larval hemolymph is correlated with leucine aminopeptidase activity, but changes in hemolymph osmotic concentration in response to environmental osmotic stress depend on the osmotic effector in the environment. Although these findings suggest that genetic and environmental factors contribute significantly toward the expression of enzymes with similar functions, a relative larval viability study of genotypes that differed significantly in dipeptidase-B (DIP-B) activity revealed that low DIP-B activity did not confer any measurable reduction in larval viability under increasing levels of environmental osmotic stress. These negative results suggest that, either DIP-B does not play a major role in osmoregulation or differential osmoregulation is not related to egg to adult viability in these tests.

scholarly journals Associations between restriction site polymorphism and enzyme activity variation for esterase 6 in Drosophila melanogaster.

Genetics ◽  
1990 ◽  
Vol 126 (4) ◽  
pp. 1021-1031 ◽  
Author(s):  
A Y Game ◽  
J G Oakeshott
Keyword(s):  
Drosophila Melanogaster ◽  
Ejaculatory Duct ◽  
Allozyme Polymorphism ◽  
Nucleotide Polymorphisms ◽  
Adult Males ◽  
Coding Region ◽  
Activity Variation ◽  
Esterase 6 ◽  
Enzyme Activity Variation ◽  
Male Activity

Abstract Thirty-five nucleotide polymorphisms were found in a 21.5-kbp region including the Est6 locus among 42 isoallelic lines extracted from a single natural population of Drosophila melanogaster. The heterozygosity per nucleotide pair was estimated to be 0.010 overall, but was lower in sequences hybridizing to transcripts than in those not hybridizing to transcripts. Eleven of 36 pairwise comparisons among the nine most common polymorphisms showed significant gametic disequilibrium. Four of these polymorphisms were also significantly associated with the major EST6-F/EST6-S allozyme polymorphism. Significant disequilibrium was generally restricted to polymorphisms less than 1-2 kbp apart. Previously reported measures of EST6 activity in virgin adult females proved not to be significantly associated with any of the six most common nucleotide polymorphisms located in the Est6 coding region or the 1.5 kbp immediately 5'. However, the 11 haplotypes for five of these polymorphisms that lie in the 1.5-kbp 5' region could explain about half of the previously reported variation among the lines for both EST6 activity and the amount of EST6 protein in virgin adult males. One particular polymorphism, for a RsaI site 530 bp 5' of the initiation codon, could explain 21% of the male activity variation among lines. This site is embedded in a large palindrome and we suggest that sequences including or close to this site may be involved in the regulation of EST6 synthesis in the ejaculatory duct of the adult male.

scholarly journals NATURALLY OCCURRING ENZYME ACTIVITY VARIATION IN DROSOPHILA MELANOGASTER. I. SOURCES OF VARIATION FOR 23 ENZYMES

Genetics ◽  
1982 ◽  
Vol 102 (2) ◽  
pp. 191-206
Author(s):  
C C Laurie-Ahlberg ◽  
A N Wilton ◽  
J W Curtsinger ◽  
T H Emigh
Keyword(s):  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Geographic Origin ◽  
Natural Populations ◽  
Genetic Component ◽  
Activity Levels ◽  
Substitution Lines ◽  
Show Evidence ◽  
Sources Of Variation ◽  
Enzyme Activity Variation

ABSTRACT The genetic component of variation of enzyme activity levels in Drosophila melanogaster was investigated by using 48 second- and 48 third-chromosome isogenic substitution lines derived from natural populations. The results confirm those of our earlier experiments with the same lines and extend them to a number of additional enzymes. All 23 enzymes show a significant genetic component to the variation in one or both sets of lines and only a small part of this variation is accounted for by variation among the lines in the amount of tissue per fly. The magnitude of line effects is, in most cases, considerably larger than the magnitude of environmental and measurement error effects, and the line effects are approximately continuous in distribution. Variation in the geographic origin and karyotype of the chromosomes generally does not contribute to the line component of variation, but allozymes provide an important source of variation for a few of the enzymes. Many of the enzymes show evidence for variation of activity modifiers that are not linked to the structural locus of the enzyme.

scholarly journals Models of quantitative variation of flux in metabolic pathways.

Genetics ◽  
1989 ◽  
Vol 121 (4) ◽  
pp. 869-876 ◽  
Author(s):  
P D Keightley
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Metabolic Pathways ◽  
Quantitative Character ◽  
Wild Type ◽  
Gene Frequencies ◽  
Activity Variation ◽  
Enzyme Activity Variation ◽  
Interaction Component ◽  
Interaction Variance

Abstract As a model of variation in a quantitative character, enzyme activity variation segregating in a population is assumed to affect the flux in simple metabolic pathways. The genetic variation of flux is partitioned into additive and nonadditive components. An interaction component of flux variance is present because the effect of an allelic substitution is modified by other substitutions which change the concentrations of shared metabolites. In a haploid population, the the proportion of interaction variance is a function of the gene frequencies at the loci contributing to the flux variation, enzyme activities of mutant and wild type at variable loci and activities at nonvariable loci. The proportion of interaction variance is inversely related to the ratio of mutant to wild-type activities at the loci controlling the enzyme activities. The interaction component as a function of gene frequencies is at a maximum with high mutant allele frequencies. In contrast, the dominance component which would apply to a diploid population is maximal as a proportion of the total when mutant alleles are at low frequencies. Unless there are many loci with large differences in activity between the alleles, the interaction component is a small proportion of the total variance. Data on enzyme activity variation from natural and artificial populations suggest that such variation generates little nonadditive variance despite the highly interactive nature of the underlying biochemical system.

Immunological evidence for structural homology between Drosophila melanogaster (S14), rabbit liver (S12), Saccharomyces cerevisiae (S25), Bacillus subtilis (S6), and Escherichia coli (S6) ribosomal proteins

1984 ◽  
Vol 4 (11) ◽  
pp. 2535-2539
Author(s):  
W Y Chooi ◽  
E Otaka
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Bacillus Subtilis ◽  
Comparative Study ◽  
Ribosomal Proteins ◽  
Rabbit Liver ◽  
Antigenic Determinants ◽  
Structural Homology ◽  
Specific Antibodies

Specific antibodies directed against Drosophila melanogaster acidic ribosomal protein S14 were used in a comparative study of eucaryotic and procaryotic ribosomes by immunoblotting and enzyme-linked immunosorbent assays. Common antigenic determinants and, thus, structural homology were found between D. melanogaster, Saccharomyces cerevisiae (S25), rabbit liver (S12), Bacillus subtilis (S6), and Escherichia coli (S6) ribosomes.

Comparative study on early digestive enzyme activity and expression in red sea bream (Pagrus major) fed on live feed and micro-diet

Aquaculture ◽  
2020 ◽  
Vol 519 ◽  
pp. 734721 ◽  
Author(s):  
Tran Nguyen Duy Khoa ◽  
Viliame Waqalevu ◽  
Akinobu Honda ◽  
Kazuhiro Shiozaki ◽  
Tomonari Kotani
Keyword(s):  
Enzyme Activity ◽  
Comparative Study ◽  
Red Sea ◽  
Digestive Enzyme ◽  
Sea Bream ◽  
Digestive Enzyme Activity ◽  
Red Sea Bream ◽  
Pagrus Major ◽  
Live Feed

scholarly journals Comparative study on glucocerebrosidase in spleens from patients with Gaucher disease

1990 ◽  
Vol 269 (1) ◽  
pp. 93-100 ◽  
Author(s):  
J M F G Aerts ◽  
W E Donker-Koopman ◽  
S Brul ◽  
S Van Weely ◽  
M C Sa Miranda ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Comparative Study ◽  
Molecular Mass ◽  
Gaucher Disease ◽  
Specific Activity ◽  
Normal Subjects ◽  
Accurate Assessment ◽  
Residual Enzyme Activity ◽  
Immunological Analysis ◽  
Immunological Method

In Gaucher disease (glucosylceramide lipidosis), deficiency of glucocerebrosidase causes pathological storage of glucosylceramide, particularly in the spleen. A comparative biochemical and immunological analysis has therefore been made of glucocerebrosidase in spleens from normal subjects (n = 4) and from Gaucher disease patients with non-neuronopathic (n = 5) and neuronopathic (n = 5) phenotypes. The spleens from all Gaucher disease patients showed markedly decreased glucocerebrosidase activity. Discrimination of different phenotypes of Gaucher disease was not possible on the basis of the level of residual enzyme activity, or by measurements, using the immunopurified enzyme, of kinetic constants, pI or molecular mass forms. A severe decrease was found in the specific activity of glucocerebrosidase purified to homogeneity from the spleen of a patient with the non-neuronopathic phenotype of Gaucher disease, as compared with that of the enzyme purified from the spleen of a normal subject. This finding was confirmed by an immunological method developed for accurate assessment of the relative enzyme activity per molecule of glucocerebrosidase protein. The method revealed that the residual enzyme in the spleens of all investigated patients with a non-neuronopathic course of Gaucher disease had a more than 7-fold decreased activity of glucocerebrosidase (measured in the presence of taurocholate) per molecule of enzyme, and that the concentration of glucocerebrosidase molecules in the spleens of these patients was near normal. Observations made with immunoblotting experiments were consistent with these findings. In contrast, in the spleens of patients with neuronopathic phenotypes of Gaucher disease, the concentration of glucocerebrosidase molecules was severely decreased.

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