Getting rid of pepsin?

[ilzmastr]

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So if enzymes are unchanged by a reaction, and after being released in their zymogen form they are irreversibly activated like pepsinogen is, how do we regulate their function?

Do they leave the stomach and get digested with the other proteins in the small intestine?

 

[jdlykins91]

So if enzymes are unchanged by a reaction, and after being released in their zymogen form they are irreversibly activated like pepsinogen is, how do we regulate their function?

Do they leave the stomach and get digested with the other proteins in the small intestine?

What do you mean by regulation of function? Regulation of presence or regulation of enyzmatic activity? After the cleavage of the pepsinogen by HCl in the stomach, it is activated and carries out its proteolytic activity. When the stomach is evacuated through the pyloric sphincter to the duodenum, the pH increases markedly due to the production of bicarbonate by the pancreas. This would result in denaturation of the protein, and thus a loss of proteolytic activity. This could then possibly expose substrate for the action of other proteases like chymotrypsin or trypsin. I am not exactly sure on that one. Then, the introduction of food would stimulate the production of hormones which would promote increased production of HCl and more pepsinogen.

 

[MedPR]

So if enzymes are unchanged by a reaction, and after being released in their zymogen form they are irreversibly activated like pepsinogen is, how do we regulate their function?

Do they leave the stomach and get digested with the other proteins in the small intestine?

Pepsin is only active at low pH. When it goes from stomach to duodenum, it gets inactivated. That's all you need to know for the MCAT.