Haemonchus contortus: characterization and purification of excretory/secretory protease(s).
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.
Kocher
D K
DK
Department of Zoology, Punjab Agricultural University, Ludhiana, India.
Ahuja
S P
SP
Sood
M L
ML
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
D007527:Isoenzymes; D010450:Endopeptidases