Isolation and some properties of an acid protease from Fasciola hepatica.
A new protease, detected in an extract of Fasciola hepatica, was isolated and partly purified. The pH optimum for the cleavage of denaturated haemoglobin by the enzyme is pH 3.0. This proteolytic activity is inhibited by diazoacetylnorleucine methyl ester, pepstatin, the pepsin inhibitor from Ascaris suum, and phenylalanine. The cathepsin D inhibitor from potatoes, EDTA, mercaptoethanol and the inorganic salts tested have no inhibitory effect. The cleavage of the B-chain of oxidized insulin by enzyme was studied and compared with the digestion of the same substrate by chicken and pig pepsin. The protease from Fasciola hepatica belongs to the carboxyl group of proteases and probably plays an important role in helminth nutrition.
D000818:Animals; D002846:Chromatography, Affinity; D005210:Fasciola hepatica / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009646:Norleucine / Q000031:analogs & derivatives / Q000494:pharmacology; D010436:Pepstatins / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D010649:Phenylalanine / Q000494:pharmacology; D011480:Protease Inhibitors; D013379:Substrate Specificity
D010436:Pepstatins; D011480:Protease Inhibitors; D010649:Phenylalanine; C000909:N-diazoacetylnorleucine methyl ester; D009646:Norleucine; D010447:Peptide Hydrolases