Identification of digestive hydrolases in the larval midgut of the camel nasal bot fly Cephalopina titillator Clark (Diptera: Oestridae).
Activities of digestive hydrolases associated with midgut of the third instar larva of Cephalopina titillator were investigated. Based on the hydrolysis of synthetic substrates and optimum pH, it was found that C. titillator midgut contains trypsin-like (optimum pH, 9), chymotrypsin esterase-like (optimum pH, 8), carboxypeptidase A and B (optimum pH at 8.5 &7 respectively), alkaline- and acid-phosphatase (optimum pH at 9 & 5 respectively) and membrane bound leucine aminopeptidase (optimum pH, 8). An acid proteinase activity was detected, by the ability to hydrolyze acid denaturated haemoglobin; and it seems to be close to pepsin than cathepsin-like enzyme. It has a maximum activity at pH- 3.5. alpha-Glucosidase activity, and was also identified (optimum pH at 6) in the midgut, and seems to be membrane bound.
Dorrah
Moataza A
MA
Department of Entomology, Faculty of Science, Cairo University, Giza, Egypt.
El-Bassiony
Ghada M
GM
D000818:Animals; D002162:Camelus / Q000469:parasitology*; D004064:Digestive System / Q000201:enzymology*; D004175:Diptera / Q000201:enzymology* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000378:metabolism*; D007814:Larva / Q000201:enzymology; D013379:Substrate Specificity
D006867:Hydrolases