What is the function of human Trypsin Inhibitor if trypsin is secreted in the inactive form of Trypsinogen?
The function of human Trypsin Inhibitor is to regulate and control the activity of trypsin in the human body. Trypsin is initially secreted as the inactive form called trypsinogen, which is converted into active trypsin by an enzyme called enterokinase. Trypsin plays a crucial role in the digestion of proteins by breaking peptide bonds between specific amino acids. However, it is important to regulate the activity of trypsin to prevent unnecessary and excessive digestion.
The human Trypsin Inhibitor acts as a defense mechanism against uncontrolled trypsin activity. It binds to trypsin and forms a stable complex, preventing its enzymatic activity. This inhibition helps to limit the activity of trypsin and maintain a balanced digestive process.
In addition to regulating trypsin activity, Trypsin Inhibitor also protects the pancreas, where trypsin is produced. The pancreas secretes both inactive trypsinogen and Trypsin Inhibitor. This ensures that trypsinogen remains inactive in the pancreas, preventing any potential self-digestion or damage to the organ.
Overall, the function of human Trypsin Inhibitor is to control trypsin activity and prevent uncontrolled digestion, maintaining a balance in the digestive process and protecting the pancreas from self-digestion.
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