Abstract
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) |
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Pages (from-to) | 4753-4761 |
Number of pages | 9 |
Journal | Journal of Biological Chemistry |
Volume | 289 |
Issue number | 8 |
DOIs | |
State | Published - Feb 21 2014 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology