Background: Initial cleavage by chymotrypsin C regulates degradation of human cationic trypsin. Results: Cleavage is reversible and favors calcium-dependent bond formation in trypsin, but not in trypsinogen. Conclusion: Trypsin resistance to degradation derives from the regulated thermodynamic stability of a specific peptide bond that is responsive to physiological environment. Significance: This new paradigm explains the robustness of trypsin functioning in the protease-rich intestinal milieu.
|Original language||English (US)|
|Number of pages||9|
|Journal||Journal of Biological Chemistry|
|State||Published - Feb 21 2014|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology