Term: trypsin
Literally meaning: “protein of rubbing”
Origin: Greek
τρίβω/trivo (=rub, powder, grind) > (simple past) ἔτριψα /etripsα
Coined/History
The enzyme
named in 1876 by Kuhne who first described an proteolytic activity of
pancreatic extract by comparing trypsin with pepsin. In 1931 J.H
Northrop purified and crystallized trypsin shortly after first purifying pepsin
(1930) and in addition to chemotrypsin (M Kunitz and JH Northrop).
Definition
Trypsin is
a proteolytic enzyme that cleaves the peptide bonds at carboxy site of residues
of lysine and arginine, except when either is followed by proline. Trypsin is
active in the duodenum and it is produced by the pancreas after the proteolysis
of proenzyme trypsinogen. Today, trypsin is used in routine protocols for cell
and tissue cultures by the process of “trypsinization”.
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, enzyme trypsin
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