Trypsin adsorption by Hymenolepis diminuta (Cestoda).
Significant amounts of radioactivity were associated with Hymenolepis diminuta following incubation in 3H-trypsin. Autoradiography of worms incubated in 3H-trypsin for 30 min demonstrated that all radioactivity was associated with the worm's surface (tegument). The amount of 3H-trypsin adsorbed by the worms was not sufficient to account for the inactivation of this enzyme in the presence of intact worms. Unlabeled trypsin and poly-L-glutamate (but not poly-L-lysine) inhibited adsorption of 3H-trypsin, but were without effect on trypsin inactivation by H. diminuta. Therefore, trypsin was adsorbed by intact H. diminuta, but the process of adsorption apparently did not play any role in inactivation of the enzyme.
D000327:Adsorption; D000818:Animals; D006926:Hymenolepis / Q000201:enzymology*; D011099:Polyglutamic Acid / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors
D014361:Trypsin Inhibitors; D011107:Polylysine; D011099:Polyglutamic Acid; D014357:Trypsin