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hydrochloric acid produced by parietal cells converts pepsin to pepsinogen
Wiki User
∙ 11y ago
Wiki User
∙ 11y agoThat would be HCl or Hydrochloric Acid.
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What are the differences between pepsin and pepsinogen?
pepsinogen makes pepsin
Is pepsin a polypeptide?
Pepsinogen is the proenzyme of pepsin. Pepsinogen is inactive, it is metabolized into the enzyme pepsin which break down proteins into small molecules.
What is chemical found in the stomach needed to activate pepsinogen to pepsin?
You think probable to pepsin or hydrochloric acid.
What is the functiom of pepsinogen?
Pepsinogen is the precursor for Pepsin, an enzyme for the degradation of protein.
What is the zymogenic form of pepsin?
pepsinogen
What is the difference between pepsin and pepsinogen?
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.
What prevents pepsin from destroying the cell walls in the stomach?
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.
What is the function of HCI?
coverts pepsinogen to pepsin Destroys bacteria
What is the inactive from of the enzyme pepsin?
The inactive form of pepsin is called pepsinogen.
What is needed for the stomach protein digesting enzymes to become active?
Zymogens are stored in their inactive form and need the Hydrochloric acid (or HCl) to be activated. Specifically, HCl converts pepsinogen into pepsin which can then be used to convert more pepsinogen into pepsin.
What are the protein hydrolyzing enzymes in the digestive tract?
pepsin, trypsin, chymotrypsin, carboxypeptidase, aminopeptidase
What enzyme start to digest proteins in the stomatch?
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.
