Kazuo Hiraizumi

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The peptidase system inDrosophila 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(More)
An examination ofDrosophila melanogaster from natural populations revealed genetic variation for dipeptidase-A (DIP-A) and dipeptidase-B (DIP-B) activities within sets of lines that differed from one another only in the second or the third chromosome. Analyses of diallel crosses indicate that both activities are inherited additively, and coordinate control(More)
Dip-A, Dip-B, andDip-C constitute structural genes for three peptidic enzymes inDrosophila melanogaster distinct from the leucine aminopeptidases. Their ontogenetic and tissue distributions of activities suggest the involvement of these enzymes in a general metabolic role, such as the regulation of amino acid and oligopeptide pools to make amino acids(More)
The enzyme dipeptidase-A (DIP-A) in Drosophila melanogaster is coded by a second chromosome locus that is polymorphic for three allozymes in natural populations. DIP-A appears to be the only enzyme in D. melanogaster capable of hydrolyzing the dipeptide glycyl-L-isoleucine, since flies homozygous for null alleles at this locus have no detectable(More)
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