DESCRIPTION
Trypsin – Trypsin 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, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream. Tryptic digestion is a necessary step in protein absorption as proteins are generally too large to be absorbed through the lining of the small intestine.Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. When the pancreas is stimulated by cholecystokinin, it is then secreted into the first part of the small intestine (the duodenum) via the pancreatic duct. Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage. Auto catalysis can happen with trypsin using trypsinogen as the substrate. This activation
MECHANISM
is common for most serine proteases, and serves to prevent autodegradation of the pancreas. Chymotrypsin – Chymotrypsin ( chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a ‘hydrophobic pocket’ (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 sidechain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine and methionine at the P1 position.
COMPOSITION
Trypsin-Chymotrypsin 100000 AU
INDICATION
Chymotrypsin is a proteolytic enzyme obtained by the activation of chymotrypsinogen extracted from the pancreas of beef that has been used in ophthalmology for the dissection of the zonule of the lens, thus facilitating intracapsular cataract extraction & reducing trauma to the eye.
PHARMACODYNAMICS
Chymotrypsin is known to interact with other drugs like alcohol, chloramphenicol. Always consult your physician for the change of dose regimen or an alternative drug of choice that may strictly be required.
No Information
FOOD INTERACTIONS
avoid alcohol
SIDE EFFECTS
Hypersensitivity reactions, corneal edema, uveitis.