title: Haemonchus contortus: characterization and purification of excretory/secretory protease(s).
abstract: The activity of protease(s) has been examined separately in excretory/secretory (E/S) products from male and female Haemonchus contortus (Nematoda: Trichostrongylidae). The E/S proteolytic activity indicated the presence of preabsorptive digestion of host blood and/or tissues. Protease 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 and female E/S products, respectively, by sequential purification with saturated ammonium sulphate followed by ion-exchange chromatography. The purification study revealed the presence of isomeric forms of protease(s) in the E/S products of H. contortus.
authors.affiliation: Department of Zoology, Punjab Agricultural University, Ludhiana, India.
authors.forename: D K
authors.initials: DK
authors.lastname: Kocher
authors.forename: S P
authors.initials: SP
authors.lastname: Ahuja
authors.forename: M L
authors.initials: ML
authors.lastname: Sood
mesh_terms: D000018:Abomasum / Q000469:parasitology; D000818:Animals; D002852:Chromatography, Ion Exchange; D004063:Digestion; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D015511:Goat Diseases / Q000469:parasitology; D006041:Goats; D006188:Haemonchiasis / Q000469:parasitology / Q000662:veterinary; D006189:Haemonchus / Q000201:enzymology* / Q000302:isolation & purification; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D008297:Male
chemical_list: D007527:Isoenzymes; D010450:Endopeptidases