Pepsin is a powerful protein digesting enzyme which is far too dangerous in its active form so it is released in an inactive pepsinogen form by the cell and activated only in the digestive tract where it is required to be active.
Pepsinogen is the proenzyme of pepsin. Pepsinogen is inactive, it is metabolized into the enzyme pepsin which break down proteins into small molecules.
Pepsinogen is an inactive precursor of the enzyme pepsin, which is responsible for breaking down proteins in the stomach. Hydrochloric acid activates pepsinogen, converting it into pepsin. The presence of hydrochloric acid in the stomach helps to create an acidic environment that allows pepsin to function optimally.
Pepsinogen is the precursor for Pepsin, an enzyme for the degradation of protein.
pepsinogen
hydrochloric acid produced by parietal cells converts pepsin to pepsinogen
Pepsinogen is activated in the stomach by the acidic environment, which triggers a change in its structure to become the active enzyme pepsin.
coverts pepsinogen to pepsin Destroys bacteria
The inactive form of pepsin is called pepsinogen.
Hydrochloric acid (HCl) is the chemical found in the stomach that is needed to activate pepsinogen to its active form, pepsin. HCl creates an acidic environment in the stomach that enables pepsinogen to undergo a conformational change and become pepsin, which is essential for protein digestion.
Pepsin is secreted as pepsinogen. Pepsinogen cannot eat the walls of the stomach. Now, pepsin is formed when pepsinogen binds to the hydrochloric acid (HCl) in the stomach. Once they are binded pepsin is formed. The second reason on why the stomach doesn't eat it's self is because of the alkaline mucus that suround the walls of the stomach.
Pepsin is produced by stomach cells in its inactive form pepsinogen, Pepsinogen is then activated by the stomach acid into its active form, pepsin. Pepsin breaks down the protein in the food into smaller particles.