Naturally occurring quantitative variants of acid phosphatase-1 in Drosophila melanogaster.
We have examined 111 wild Drosophila melanogaster lines for cis-acting quantitative variants of the Acph-1 gene, which codes for acid phosphatase-1 (ACPH). Three variants with obvious, reproducible phenotypes were isolated. All variants acted equally on all tissues and developmental stages examined. No recombinants were detected between one quantitative variant and the site determining the electrophoretic mobility of Acph-1 among 3885 flies examined. Several enzymatic properties of the variant enzymes were tested, including the Km values for two substrates, inhibition by three different inhibitors, and thermal stability; the variant enzymes behaved identically to the wild-type enzyme in all cases. Immunological titration experiments showed that the variant enzymes had the same enzyme activity per molecule of ACPH as the wild-type enzyme. These results suggest that the quantitative variants we have identified are altered in the regulatory portion of Acph-1 so as to produce altered numbers of normal ACPH molecules.
D000135:Acid Phosphatase / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D003433:Crosses, Genetic; D003434:Crossing Over, Genetic; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics; D005260:Female; D005796:Genes; D008040:Genetic Linkage; D014644:Genetic Variation; D005779:Immunodiffusion; D007700:Kinetics; D008297:Male
D000135:Acid Phosphatase