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Gastrin secretes what?

pepsinogen (a precursor of pepsin) which helps humans digest, when activated by HCL.


What is the source of pepsin?

Pepsin is an enzyme which is secreted by Zymogen cells of the stomach. First it is secreted in an inactive form called Pepsinogen. After that Hydrochloric acid (HCl) activates it into pepsin. FUNCTION:Its function is to hydrolyse the proteins to yield peptide.


What is the inactive precursor of pepsin?

The inactive precursor of pepsin is called pepsinogen. It is secreted by the gastric chief cells in the stomach lining and is activated to pepsin in the presence of hydrochloric acid (HCl) in the gastric environment. This activation process prevents the enzyme from digesting the proteins in the cells that produce it. Pepsin then plays a crucial role in protein digestion by breaking down complex proteins into smaller peptides.


Where is Gastric Protease located?

Gastric protease, primarily pepsin, is located in the stomach. It is secreted by the gastric glands as an inactive precursor called pepsinogen, which is activated by the acidic environment of gastric juice. This enzyme plays a crucial role in the digestion of proteins, breaking them down into smaller peptides.


What is the inactive from of the enzyme pepsin?

The inactive form of pepsin is called pepsinogen.


What is the site of pepsin production?

Pepsin is produced in the stomach, specifically by the chief cells located in the gastric glands of the gastric mucosa. It is secreted as an inactive precursor called pepsinogen, which is activated to pepsin in the presence of gastric acid (hydrochloric acid). This activation occurs in the acidic environment of the stomach, enabling pepsin to play its role in protein digestion.


Why is pepsin not produced straight away(without the presence of food)?

Pepsin is not produced immediately because it is secreted as an inactive precursor called pepsinogen, which protects the gastric mucosa from being digested by its own enzyme. The production of pepsinogen is stimulated by the presence of food in the stomach, along with hormonal signals. This mechanism ensures that pepsin is activated only when needed, preventing premature digestion of stomach lining and reducing potential damage to the gastrointestinal tract.


Why can pepsin not be produced in its active form?

Pepsin degrades proteins so if it was active it would immediately begin digesting all the proteins in the cell. Therefore it is produced from a precursor known as a zymogen or proenzyme. Pepsin's proenzyme form is pepsinogen which is transformed to the activated pepsin protein.


What is the gastric enzyme that acts on proteins?

The proteolytic or protein eating enzyme of the stomach is called pepsin. Pepsin is secreted into the stomach as a zymogen (or inactive enzyme precursor) called pepsinogen which is converted into the active enzyme form by the hydrochloric acid and low pH in the gastric juices.


What is the name of the inactive form of a protein splitting enzyme in the stomach?

The inactive form of a protein splitting enzyme in the stomach is called pepsinogen. It gets converted to its active form, pepsin, when exposed to the acidic environment of the stomach.


Which enzyme secreted from gastric gland in stomach that acts on protein?

The enzyme secreted from the gastric gland in the stomach that acts on proteins is pepsin. It is produced in an inactive form called pepsinogen, which is activated by hydrochloric acid (HCl) in the stomach. Pepsin breaks down proteins into smaller peptides, facilitating protein digestion.


What enzyme is produced in the stomach and breaks some of the peptide bonds in polypeptide chains?

The enzyme produced in the stomach that breaks some of the peptide bonds in polypeptide chains is called pepsin. It is secreted by the stomach lining as an inactive precursor, pepsinogen, which is activated by the acidic environment of the stomach. Pepsin plays a crucial role in the digestion of proteins, breaking them down into smaller peptides for further digestion in the small intestine.