Find, compare & contact
Chymotrypsin API Manufacturers & Suppliers

General Description:

Chymotrypsin, identified by CAS number 9004-07-3, is a notable compound with significant therapeutic applications. 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 . 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 .

Indications:

This drug is primarily indicated for: No therapeutic indications. Its use in specific medical scenarios underscores its importance in the therapeutic landscape.

Metabolism:

Chymotrypsin undergoes metabolic processing primarily in: No pharmacokinetic data available. This metabolic pathway ensures efficient processing of the drug, helping to minimize potential toxicity and side effects.

Absorption:

The absorption characteristics of Chymotrypsin are crucial for its therapeutic efficacy: No pharmacokinetic data available. The drug's ability to rapidly penetrate into cells ensures quick onset of action.

Half-life:

The half-life of Chymotrypsin is an important consideration for its dosing schedule: No pharmacokinetic data available. This determines the duration of action and helps in formulating effective dosing regimens.

Protein Binding:

Chymotrypsin exhibits a strong affinity for binding with plasma proteins: No pharmacokinetic data available. This property plays a key role in the drug's pharmacokinetics and distribution within the body.

Route of Elimination:

The elimination of Chymotrypsin from the body primarily occurs through: No pharmacokinetic data available. Understanding this pathway is essential for assessing potential drug accumulation and toxicity risks.

Volume of Distribution:

Chymotrypsin is distributed throughout the body with a volume of distribution of: No pharmacokinetic data available. This metric indicates how extensively the drug permeates into body tissues.

Clearance:

The clearance rate of Chymotrypsin is a critical factor in determining its safe and effective dosage: No pharmacokinetic data available. It reflects the efficiency with which the drug is removed from the systemic circulation.

Pharmacodynamics:

Chymotrypsin exerts its therapeutic effects through: 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. The drug's ability to modulate various physiological processes underscores its efficacy in treating specific conditions.

Mechanism of Action:

Chymotrypsin functions by: 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. This mechanism highlights the drug's role in inhibiting or promoting specific biological pathways, contributing to its therapeutic effects.

Toxicity:

Categories:

Chymotrypsin is categorized under the following therapeutic classes: Blood and Blood Forming Organs, Endopeptidases, Enzymes, Enzymes and Coenzymes, Hydrolases, Ophthalmologicals, Peptide Hydrolases, Sensory Organs, Serine Endopeptidases, Serine Proteases, Surgical Aids. These classifications highlight the drug's diverse therapeutic applications and its importance in treating various conditions.