Characterization and purification of cytosolic and membrane-bound protease(s) in adults of Haemonchus contortus.
The activity of protease(s) was observed separately in cytosolic and membrane-bound protease(s) from male and female Hae monchus contortus (Nematoda: Trichostrongylidae). Different fractions showed optimum protease activity at 37 degrees C, pH 8.5 and 8.0 mg casein concentration. The female fractions had a particularly high activity of protease(s) in comparison with the male fractions, especially of membrane-bound enzymes in the anterior half. Inhibition, activation studies revealed the presence of four kinds of protease(s) in cytosolic and membrane-bound fractions. Protease(s) in different fractions are purified to a greater extent by higher concentrations of saturated ammonium sulphate solution, i.e. ranging from 50 to 65%. The purification study revealed the presence of multiple forms of protease(s) in cytosolic and membrane-bound extracts of H. contortus.
Kocher
D K
DK
Department of Zoology, Punjab Agricultural University, Ludhiana, India.
Ahuja
S P
SP
Sood
M L
ML
D000818:Animals; D010450:Endopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006189:Haemonchus / Q000201:enzymology*; D008297:Male; D012727:Sex Characteristics
D010450:Endopeptidases