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In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.
Chief cells are part of fundic gland polyps (here shown in high magnification). [11]In gastric tissue, a loss of parietal cells due to chronic inflammation has been shown to affect chief cell differentiation and can induce chief cells to transdifferentiate back into neck cells and can lead to the formation of mucus cell metaplasia known as spasmolytic polypeptide expressing metaplasia (SPEM ...
Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the ...
A gastric chief cell, peptic cell, or gastric zymogenic cell is a type of gastric gland cell that releases pepsinogen and gastric lipase.It is the cell responsible for secretion of chymosin (rennin) in ruminant animals and some other animals. [1]
Protein C, also known as autoprothrombin IIA and blood coagulation factor XIV, [5]: 6822 [6] is a zymogen, that is, an inactive enzyme.The activated form plays an important role in regulating anticoagulation, inflammation, and cell death and maintaining the permeability of blood vessel walls in humans and other animals.
Thomas Jefferson University is apologizing after the names of some graduates from the nursing program were unrecognizably pronounced at their commencement, as seen in videos from the ceremony that ...
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
Chymotrypsinogen. Chymotrypsinogen is an inactive precursor of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides. Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. [1]