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Acetylcholinesterase secretion by parasitic nematodes. I. Evidence for secretion of the enzyme by a number of species


, : Acetylcholinesterase secretion by parasitic nematodes. I. Evidence for secretion of the enzyme by a number of species. International Journal for Parasitology 3(5): 589-597

Studies made on the acetylcholinesterase of the parasitic stages of Trichostrongylus colubriformis, T. axei, Oesophagostomum venulosum, Ostertagia circumcincta, Chabertia ovina and Haemonchus contortus from sheep, Oesophagostomum radiatum, Cooperia pectinata and H. placei from calves, Nippostrongylus brasiliensis from rat and Nematospiroides dubius from mouse revealed levels ranging from 80 and 84 mu moles of acetylthiocholine hydrolysed/g/hour for H. placei and C. pectinata adults, respectively, to 22,976 mu moles/g/hour for 4th-stage T. colubriformis. Little of the activity was due to pseudocholinesterase, and 41 to 64% of the enzyme was soluble except for C. pectinata, H. contortus adults and all the infective larvae studied, which all had less than 20% soluble enzyme. T. colubriformis, T. axei, O. radiatum and O. venulosum had high total levels of acetylocholinesterase, much of it soluble and apparently located in the oesophageal and/or excretory glands, and showed high rates of enzyme release in vitro; Ostertagia circumcincta and Chabertia ovina showed moderate rates of enzyme release, and Cooperia pectinata very low rates. A study of the kinetics of inhibition of acetylcholinesterase activity in the soluble extract of Nippostrongylus brasiliensis using coroxon, together with acrylamide gel electrophoresis, provided evidence for 2 different types of the enzyme differing in sensitivity to the inhibitor.

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PMID: 4795374


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