An aspartic proteinase in Drosophila: maternal origin and yolk localization.
An aspartic proteinase activity has been found in Drosophila oocytes and embryos. The proteinase is maximally active at pH 3.5 and has been characterized by its sensitivity to specific inhibitors and by the specificity of cleavage. The activity is very low and has been localized in the yolk granules. The proteinase is detected in mature oocytes (i.e., it is of maternal origin) and remains essentially constant during embryogenesis. This suggests that the Drosophila aspartic proteinase functions mainly before embryogenesis.
Medina
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M
Instituto de Investigaciones Biomédicas del CSIC, Facultad de Medicina, Universidad Autónoma de Madrid, Spain.
Vallejo
C G
CG
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000196:embryology* / Q000201:enzymology; D004527:Egg Proteins / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000201:enzymology; D010450:Endopeptidases / Q000378:metabolism*; D009865:Oocytes / Q000201:enzymology; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
D004527:Egg Proteins; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D