Inactivation of alpha- and beta-chymotrypin by intact Hymenolepis diminuta (Cestoda).

Abstract

When specimens of intact Hymenolepis diminuta were incubated in the presence of α- or β-chymotrypsin, assays for proteolytic activity following removal of the worms showed an inactivation of both enzymes. The amount of inactivation in either case was dependent upon the enzyme concentration, total number of worms (total worm weight) present, period of time worms were incubated with the enzymes, and pH of the assay medium. Inactivation of α- and β-chymotrypsin was independent of available surface area and the presence of polyions, was irreversible, and ceased upon removal of the worms from the medium. Intact worms also inactivited the zymogen, α-chymotrypsinogen A. The data suggest that the inactivation of α- and β-chymotrypsin resembles that previously reported for inactivation of trypsin by intact H. diminuta.