HAEMONCHUS-CONTORTUS - CHARACTERIZATION AND PURIFICATION OF EXCRETORYSECRETORY PROTEASE(S)/

The activity of protease(s) has been examined separately in excretory/ secretory (E/S) products from male and female Haemonchus contorius (Ne matoda: Trichostrongylidae). The E/S proteolytic activity indicated th e presence of preabsorptive digestion of host blood and/or tissues. Pr otease activity was optimum at 37 degrees C, pH 8.5 and 8.0 mg casein. These protease(s) were purified to 32.16- and 88.80-folds from male a nd female E/S products, respectively, by sequential purification with saturated ammonium sulphate followed by ion-exchange chromatography. T he purification study revealed the presence of isomeric forms of prote ase(s) in the E/S products of H. contortus.