The activity of protease(s) has been examined separately in excretory/secretory (E/S) products from male and female Haemombus mntorhrs (Nematoda: Trichostron lidae). The E/S proteolytic activity indicated the presence of preabsorptive digestion of host blood andEr tissues. Protease activity was optimum at 37OC, 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. contorhvs.
The activity of protease(s) has been observed separately in male and female Tncburis globdosa. Different fractions showed optimum protease activity at 37OC, pH 9.5 and 1.5 mg casein concentration. Excretory/secretory @/S) products showed maximum protease activity, which might be helpful in the degradation of mucosal tissue of the host gut. Male parasites appear to feed extensively on connective tissue collagen/elastin, while females feed on both connective tissue and body/cellular fluids. Inhibition/activation studies revealed the presence of four kinds of protease in the E/S products, cytosolicand membrane-bound fractions performing different functions.
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