Pancrelipase protease API Manufacturers

General Description:

Pancrelipase protease, identified by CAS number 9001-94-9, is a notable compound with significant therapeutic applications. Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands. The pancrelipase protease is a mix of enzymes, formed by trypsin and chymotrypsin, that proteolytically cleave peptide bonds and are involved in food digestion. The pancrelipase mixture, including pancrelipase protease, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.

Indications:

This drug is primarily indicated for: Please refer to . Its use in specific medical scenarios underscores its importance in the therapeutic landscape.

Metabolism:

Pancrelipase protease undergoes metabolic processing primarily in: Please refer to . This metabolic pathway ensures efficient processing of the drug, helping to minimize potential toxicity and side effects.

Absorption:

The absorption characteristics of Pancrelipase protease are crucial for its therapeutic efficacy: Please refer to . The drug's ability to rapidly penetrate into cells ensures quick onset of action.

Half-life:

The half-life of Pancrelipase protease is an important consideration for its dosing schedule: Please refer to . This determines the duration of action and helps in formulating effective dosing regimens.

Protein Binding:

Pancrelipase protease exhibits a strong affinity for binding with plasma proteins: Please refer to . This property plays a key role in the drug's pharmacokinetics and distribution within the body.

Route of Elimination:

The elimination of Pancrelipase protease from the body primarily occurs through: Please refer to . Understanding this pathway is essential for assessing potential drug accumulation and toxicity risks.

Volume of Distribution:

Pancrelipase protease is distributed throughout the body with a volume of distribution of: Please refer to . This metric indicates how extensively the drug permeates into body tissues.

Clearance:

The clearance rate of Pancrelipase protease is a critical factor in determining its safe and effective dosage: Please refer to . It reflects the efficiency with which the drug is removed from the systemic circulation.

Pharmacodynamics:

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

Mechanism of Action:

Pancrelipase protease functions by: Pancrelipase protease acts on the peptide bonds within the proteins. The two constituents of the pancrelipase protease, trypsin, and chymotrypsin, are grouped under the family of serine proteases. Trypsin acts on lysine and arginine residues while chymotrypsin acts in hydrophobic residues such as tryptophan, tyrosine and phenylalanine. Both constituents present a catalytic site in the S1 binding pocket formed by a triad of serine, histidine and aspartate. This mechanism highlights the drug's role in inhibiting or promoting specific biological pathways, contributing to its therapeutic effects.

Toxicity:

Classification:

Pancrelipase protease belongs to the None, classified under the direct parent group Peptides. This compound is a part of the Organic Compounds, falling under the Organic Acids superclass, and categorized within the Carboxylic Acids and Derivatives class, specifically within the Amino Acids, Peptides, and Analogues subclass.

Categories:

Pancrelipase protease is categorized under the following therapeutic classes: Enzymes, Enzymes and Coenzymes, Hydrolases, Peptide Hydrolases. These classifications highlight the drug's diverse therapeutic applications and its importance in treating various conditions.

Experimental Properties:

Further physical and chemical characteristics of Pancrelipase protease include:

• Water Solubility: 1 mg/ml