Chymotrypsin A
Chymotrypsin A Uses, Dosage, Side Effects, Food Interaction and all others data.
Chymotrypsin A (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 A is the most abundant pancreatic proteases that represent up to 10-20% of the total protein synthesized by the exocrine pancreas . Chymotrypsin A contains both the catalytic triad and oxyanion hole, and the tertiary structure of chymotrypsin is similar to Trypsin .
Chymotrypsin A 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.
| Trade Name | Chymotrypsin A |
| Generic | Chymotrypsin |
| Chymotrypsin Other Names | alpha-Chymotrypsin, Chymotrypsin, Chymotrypsin A, Chymotrypsin B, Chymotrypsine, Chymotrypsinum, Quimotripsina |
| Type | |
| Protein binding | No pharmacokinetic data available. |
| Groups | Approved, Vet approved |
| Therapeutic Class | |
| Manufacturer | |
| Available Country | |
| Last Updated: | September 19, 2023 at 7:00 am |
Uses
Chymotrypsin A 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.
Chymotrypsin A 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 Chymotrypsin A works
Chymotrypsin A 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 A, which is a more stable form than π-Chymotrypsin A. 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 A favors aromatic residues like phenylalanine, tyrosine, and tryptophan but may hydrolyze other bonds in peptides at slower rates.
Toxicity
No toxicokinetic data available.
Food Interaction
- Take with food.
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.
Innovators Monograph
You find simplified version here Chymotrypsin A
FAQ
What is Chymotrypsin A used for?
People use Chymotrypsin A to make medicine. People take Chymotrypsin A by mouth or as a shot to reduce redness and swelling associated with pockets of infection (abscesses), ulcers, surgery, or traumatic injuries; and to help loosen phlegm in asthma, bronchitis, lung diseases, and sinus infections.
How safe is Chymotrypsin A?
Chymotrypsin A is safe when used in the eye by a healthcare professional. Chymotrypsin A can cause side effects when used in the eye, including an increase in pressure in the eye and other eye conditions such as uveitis, paralysis of the iris, and keratitis.
How does Chymotrypsin A work?
Chymotrypsin A cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.
What are the common side effects of Chymotrypsin A?
Common side effects of Chymotrypsin A include are itching, shortness of breath, swelling of the lips or throat, shock, loss of consciousness, and death.
Is Chymotrypsin A safe during pregnancy?
Not enough is known about the use of Chymotrypsin A during pregnancy. Stay on the safe side and avoid use.
Is Chymotrypsin A safe during breastfeeding?
You should not breastfeed while taking this medicine. You should consult your doctor before using this medicine during breastfeeding.
Can I drink alcohol with Chymotrypsin A?
Interaction with alcohol is unknown. It is advisable to consult your doctor before consumption.
Who should not take Chymotrypsin A?
Avoid Chymotrypsin A if you have any allergies to it. Seek immediate medical attention if you notice any symptoms such as a skin rash, itching/swelling (especially of the face/tongue/throat), severe dizziness, breathing difficulty, etc.
What happen If I missed Chymotrypsin A?
If you forget to take a dose of Chymotrypsin A, take it as soon as you remember. If you miss a scheduled dose, skip the missed dose. Do not double the dose to make up for the missed one.
Can I overdose on Chymotrypsin A?
You should not take more than the prescribed dose. Seek emergency medical attention or contact your doctor in case of an overdose with Chymotrypsin A.
When should be taken of Chymotrypsin A?
Chymotrypsin A is most effective when you take it 30 minutes before a meal. Swallow the tablet whole with a sufficient amount of water.
How long does Chymotrypsin A take to work?
Some people may notice an improvement within three to seven days when taking Chymotrypsin A.
Can I take Chymotrypsin A for a long time?
Chymotrypsin A is possibly safe for most people when mixed with trypsin and used short-term.
How much Chymotrypsin A can I take daily?
Doses up to 800,000 units per day of this combination have been used safely for up to 10 days.
Is Chymotrypsin A an inhibitor?
Many food plants contain one or more protease inhibitors (e.g. chymotrypsin or trypsin inhibitors) that competitively inhibit the activity of proteolytic enzymes.
