Ambezim
Ambezim Uses, Dosage, Side Effects, Food Interaction and all others data.
Chymotrypsin (EC 3.4.21.1) is a digestive enzyme that promotes proteolysis, or the breakdown of proteins and polypeptides. It is a serine protease synthesized in the pancreas and is a vital component in the pancreatic juice. Like most proteolytic enzymes, chymotrypsin is activated from its inactive zymogen precursor, chymotrypsinogen, in presence of Trypsin. Chymotrypsin is the most abundant pancreatic proteases that represent up to 10-20% of the total protein synthesized by the exocrine pancreas . Chymotrypsin contains both the catalytic triad and oxyanion hole, and the tertiary structure of chymotrypsin is similar to Trypsin .
Chymotrypsin is a digestive enzyme synthesized in the pancreas that plays an essential role in proteolysis, or the breakdown of proteins and polypeptides. As a component in the pancreatic juice, chymotrypsin aids in the digestion of proteins in the duodenum by preferentially cleaving peptide amide bonds.
Trypsin is a serine protease that plays an essential role in protein hydrolysis and absorption in mammals. When converted from its zymogen trypsinogen, trypsin is available as an active peptide hydrolase (EC 3.4.21.4) form to cleave peptide chains, mainly at the carboxyl side of the amino acids lysine or arginine. Trypsin contains a nucleophilic residue Ser in the enzyme active site which attacks the carbonyl moiety of the substrate peptide bond to form an acyl-enzyme intermediate . This nucleophilic attack is facilitated by the catalytic triad consisting of histidine-57, aspartate-102, and serine-195. Trypsin also contains an oxyanion hole that stabilizes the charge negative charge on the carbonyl oxygen atom formed from the cleavage of peptide bonds. Therapeutic forms of trypsin is obtained from purified extracts of porcine or bovine pancreas and is intended to aid in digestion when administered orally.
Trade Name | Ambezim |
Generic | Chymotrypsin + Trypsin |
Type | |
Therapeutic Class | |
Manufacturer | |
Available Country | |
Last Updated: | September 19, 2023 at 7:00 am |
Uses
Chymotrypsin is a digestive enzyme supplement used as supportive therapy to manage the side effects associated with conventional chemotherapy, radiotherapy, and hormone therapy.
No therapeutic indications.
Trypsin is a naturally occurring proteolytic enzyme found in the digestive tract of mammals. Used clinically in combination with bromelain and rutosides in the treatment of some inflammatory conditions.
Ambezim is also used to associated treatment for these conditions: Colorectal Cancers, Head & Neck Squamous Cell Carcinoma, Locally Advanced Cervical Cancer, Locally Advanced Non-Small Cell Lung Cancer, Multiple Myeloma (MM), Primary Non-metastatic Breast CancerInflammatory Reaction of the genitourinary tract, Osteoarthritis (OA), Thrombophlebitis, Traumatic Injuries, Localized soft tissue rheumatism
How Ambezim works
Chymotrypsin is synthesized by pancreatic acinar cells as an inactive precursor, chymotrypsinogen, that is secreted to the duodenum and activated via trypsin-induced cleavage. It also induces its own activation by cleaving essential amino acid residues in the oxyanion hole to produce α-Chymotrypsin, which is a more stable form than π-Chymotrypsin. Residues His-57, Asp-102, and Ser-195 form the catalytic triad while residues 189–195, 214–220, and 225–228 form the primary substrate-binding pocket called S1 binding pocket . Residue 189 in the polar serine residue that lies at the bottom of the S1 binding pocket . Chymotrypsin favors aromatic residues like phenylalanine, tyrosine, and tryptophan but may hydrolyze other bonds in peptides at slower rates.
Toxicity
No toxicokinetic data available.
Volume of Distribution
No pharmacokinetic data available.
Elimination Route
No pharmacokinetic data available.
Half Life
No pharmacokinetic data available.
Clearance
No pharmacokinetic data available.
Elimination Route
No pharmacokinetic data available.
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