Tryprol

Tryprol 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.

Tryprol
Uses
Dosage
Side Effect
Precautions
Interactions
Uses during Pregnancy
Uses during Breastfeeding
Accute Overdose
Food Interaction
Half Life
Volume of Distribution
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Interaction With other Medicine
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Trade Name	Tryprol
Generic	Chymotrypsin + Trypsin (Protease)
Weight	50000iu
Type	Tablet
Therapeutic Class
Manufacturer	Unexo Labs (pvt) Ltd,
Available Country	Pakistan
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.

Tryprol 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 Cancer

How Tryprol 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.