Let me share with you a difference between trypsin and trypsinogen.
| Aspect | Trypsin | Trypsinogen |
| Introduction | Trypsin catalyzes the hydrolysis of peptide bonds in proteins | Trypsinogen is the inactive precursor form of trypsin |
| Produced by | Synthesized and released by the pancreas as trypsinogen | Synthesized and released by the pancreas as an inactive zymogen (proenzyme) |
| Activation | Activated in the small intestine, particularly in the duodenum | Typically activated within the pancreas before release into the small intestine |
| Activation mechanism | Activated by enteropeptidase (enterokinase), an enzyme in the brush border of the small intestine | Activated by the removal of a specific peptide segment by another enzyme, trypsin |
| pH range | Functions optimally in a slightly basic pH environment | The conversion of trypsinogen to trypsin is initiated in the alkaline environment of the small intestine |
| Associated Conditions | Dysregulation or dysfunction may contribute to digestive disorders like pancreatitis | Dysfunction may contribute to impaired protein digestion and absorption in the small intestine |