Chromosomal effects on peptidase activities in Drosophila melanogaster

The peptidase system in Drosophila melanogaster (dipeptidase-A, -B, and -C and leucine aminopeptidases G and P) was used as a model to study the effects of modifier genes on activity of enzymes with similar functions. A screen of X, second, and third chromosome substitution isogenic lines revealed t...

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Bibliographic Details
Published in:Biochemical genetics 1993-02, Vol.31 (1-2), p.29-50
Main Authors: HIRAIZUMI, K, MATHES, K. D, SHALISH, C. I
Format: Article
Language:English
Subjects:
Analysis of Variance
Animals
Biological and medical sciences
Chromatography, Ion Exchange
Chromosomes - physiology
Classical genetics, quantitative genetics, hybrids
Dipeptidases - genetics
Dipeptidases - isolation & purification
Dipeptidases - metabolism
Drosophila melanogaster
Drosophila melanogaster - enzymology
Drosophila melanogaster - genetics
Fundamental and applied biological sciences. Psychology
Genetic Variation
Genetics of eukaryotes. Biological and molecular evolution
Invertebrata
Leucyl Aminopeptidase - genetics
Leucyl Aminopeptidase - isolation & purification
Leucyl Aminopeptidase - metabolism
Male
X Chromosome - physiology
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Summary:The peptidase system in Drosophila melanogaster (dipeptidase-A, -B, and -C and leucine aminopeptidases G and P) was used as a model to study the effects of modifier genes on activity of enzymes with similar functions. A screen of X, second, and third chromosome substitution isogenic lines revealed the presence of activity modifiers for peptidases on all three chromosomes. Correlation analyses indicated that covariation between some of the peptidase activities is independent of genetic background, while others are associated with variable second chromosomes. Chromosome-specific effects on Km, Vmax, and specific activity of partially purified peptidases were also detected. Moreover, a repeatable technique using anion-exchange column chromatography allowed the characterization of possibly two putative peptidic enzymes, glycyl-L-isoleucine-ase and L-leucyl-L-proline-ase, whose kinetic properties differ from the dipeptidases and the leucine aminopeptidases. These findings confirm the existence of activity modifiers for peptidases, much like other enzymes in Drosophila melanogaster.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF02399818