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Trypsin adsorption by Hymenolepis diminuta (Cestoda)
The Journal of Parasitology
|February 1, 1980
Summary
Hymenolepis diminuta adsorbs radioactive 3H-trypsin onto its surface (tegument). However, this adsorption does not explain the worm's ability to inactivate the enzyme.
Area of Science:
- Biochemistry
- Parasitology
- Molecular Biology
Background:
- Hymenolepis diminuta is a tapeworm parasite.
- Trypsin is a digestive enzyme crucial for protein breakdown.
Purpose of the Study:
- To investigate the interaction between Hymenolepis diminuta and trypsin.
- To determine if trypsin adsorption by the worm is responsible for its inactivation.
Main Methods:
- Incubation of H. diminuta with radiolabeled 3H-trypsin.
- Autoradiography to visualize radioactivity localization.
- Inhibition assays using unlabeled trypsin and poly-amino acids.
Main Results:
- Radioactivity from 3H-trypsin was localized to the H. diminuta tegument.
- Trypsin adsorption was inhibited by unlabeled trypsin and poly-L-glutamate.
- Adsorption did not correlate with trypsin inactivation by the worms.
Conclusions:
- Hymenolepis diminuta adsorbs trypsin onto its surface.
- The mechanism of trypsin inactivation by H. diminuta is independent of surface adsorption.