Trypsin
Samson-Med OAO
974 Items
2019-09-19
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Clinical Pharmacology
Trypsin - proteolytic.
Pharmacodynamics
Optimum action at pH 7–9. When applied topically, it has anti-inflammatory, regenerating and necrolitic effects. Lyses necrotic tissue and fibrous formations, promotes rejection of necrotic tissue, dilutes pus and facilitates its separation, improves the process of wound regeneration. Does not cause changes in the hemostatic system. In relation to healthy tissues, it is inactive and safe due to the presence of trypsin inhibitors (specific and nonspecific) in them.
Indications
- Bronchiectasis,
- lung abscesses,
- exudative pleurisy,
- postoperative atelectasis,
- pleural empyema;
- treatment of purulent wounds and burns;
- chronic suppurative otitis
- purulent sinusitis,
- sinusitis;
- acute thrombophlebitis,
- acute and chronic odontogenic osteomyelitis,
- inflammatory-dystrophic forms of periodontal disease,
- acute iridium and iridocyclitis,
- hemorrhages in the chamber of the eye and edema of the orbital tissues after injuries and operations,
- obstruction of tears.
Composition
1 bottle contains:
Active substance: trypsin (cattle pancreas) 10 mg.
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Dosage and Administration
Intramuscularly. Adults - 5-10 mg 1-2 times a day; children - 2.5 mg once a day. For injection, immediately before use, 5 mg of crystalline trypsin is diluted in 1-2 ml of 0.9% NaCl solution or 0.5-2% procaine solution. The course of treatment is 6-15 injections. Electrophoresis with trypsin is also used: for 1 procedure 10 mg of trypsin (dissolve in 15–20 ml of distilled water) is injected from the negative pole.
Inhalation: 5-10 mg in 2-3 ml of 0.9% NaCl solution through an inhaler or through a bronchoscope. After inhalation, rinse your mouth with warm water and rinse your nose.
Eye drops: conjunctival, 0.2–0.25% solution, which is prepared immediately before use.
Intrapleural: once a day, 10–20 mg, dissolved in 20–50 ml of 0.9% NaCl solution.
Intrapleural: 50–150 mg in 5–30 ml of phosphate buffered saline, after administration, frequent changes in body position are desirable; on the 2nd day after instillation, as a rule, a liquefied exudate is released.
Locally: A three-layer tissue made of dialdehyde cellulose, impregnated with trypsin solution, is applied to the wound (after its treatment) and fixed with a bandage, left on the wound for no more than 24 hours. Before use, the cloth is moistened with distilled water or furacilin solution. The time for complete cleansing of the wound from necrotic tissue and pus is 24–72 hours. If necessary, apply again.
Inhalation: 5-10 mg in 2-3 ml of 0.9% NaCl solution through an inhaler or through a bronchoscope. After inhalation, rinse your mouth with warm water and rinse your nose.
Eye drops: conjunctival, 0.2–0.25% solution, which is prepared immediately before use.
Intrapleural: once a day, 10–20 mg, dissolved in 20–50 ml of 0.9% NaCl solution.
Intrapleural: 50–150 mg in 5–30 ml of phosphate buffered saline, after administration, frequent changes in body position are desirable; on the 2nd day after instillation, as a rule, a liquefied exudate is released.
Locally: A three-layer tissue made of dialdehyde cellulose, impregnated with trypsin solution, is applied to the wound (after its treatment) and fixed with a bandage, left on the wound for no more than 24 hours. Before use, the cloth is moistened with distilled water or furacilin solution. The time for complete cleansing of the wound from necrotic tissue and pus is 24–72 hours. If necessary, apply again.
Adverse reactions
- Allergic reactions.
- Increased body temperature, tachycardia .
- Soreness and hyperemia at the injection site after intramuscular injection.
- Inhalation of trypsin may cause irritation of the mucous membranes of the upper respiratory tract and hoarseness.
Special instructions
Do not inject the drug into the foci of inflammation and bleeding cavities. Do not administer the drug intravenously. Trypsin should not be applied to the ulcerated surfaces of malignant tumors in order to avoid the spread of the malignant process.
- Brand name: Trypsin
- Active ingredient: Trypsin
- Dosage form: Lyophilisate for preparation of solution for injections and local application
- Manufacturer: Samson-Med OAO
- Country of Origin: Russia
Studies and clinical trials of Trypsin (Click to expand)
- Inter-C? atomic potentials derived from the statistics of average interresidue distances in proteins: Application to bovine pancreatic trypsin inhibitor
- Urea and Heat Unfolding of Cold-Adapted Atlantic Cod(Gadusmorhua) Trypsin and Bovine Trypsin
- Low Trypsin and Chymotrypsin Inhibitor Mutants in Winged Bean(Psophocarpus tetragonolobus (L) DC)
- Proteinaceous Inhibitors of Trypsin and of Amylases in Developing and Germinating Seeds of Pigeon Pea (Cajanus cajan(L) Millsp)
- Response of pancreatic secretions to feeding diets with low and high levels of soybean trypsin inhibitors in growing pigs
- Response of nutrient digestibilities to feeding diets with low and high levels of soybean trypsin inhibitors in growing pigs
- Effect of condensed tannins prepared from several forages on thein vitro precipitation of ribulose-1,5-bisphosphate carboxylase (Rubisco) protein and its digestion by trypsin (EC 2.4.21.4) and chymotrypsin (EC 2.4.21.1)
- Isolation and characterisation of four trypsin-chymotrypsin inhibitors from lentil seeds
- Modelling of the inactivation kinetics of the trypsin inhibitors in soy flour
- Genotype � environment influence on cowpea (Vigna unguiculata (L) walp) antinutritional factors: 1 - trypsin inhibitors, tannins, phytic acid and haemagglutinin
- Studies on the biological responses of rats to seed trypsin inhibitors using near-isogenic lines ofPisum sativum L (pea)
- Genetic regulation of trypsin inhibitory activity in soybean flour
- Proximate composition, amino acid content and haemagglutinating and trypsin-inhibiting activities of some BrazilianVigna unguiculata (L) Walp cultivars
- Compact exocrine pancreas of ammocoetes of the southern hemisphere lampreyMordacia mordax contains a trypsin inhibitor: Putative evolutionary considerations
- Treatment ofXenopus laevis coelomic eggs with trypsin mimics pars recta oviductal transit by selectively hydrolyzing envelope glycoprotein gp43, increasing sperm binding to the envelope, and rendering eggs fertilizable
- Synthesis and Characterization of an Acrylamide-based Water-soluble Affinity Polymer for Trypsin Purification
- Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: A molecular dynamics study
- Modeling of serpin-protease complexes: Antithrombin-thrombin, α1-antitrypsin (358Met→Arg)-thrombin, α1-antitrypsin (358Met→Arg)-trypsin, and antitrypsin-elastase
- Crystallization and preliminary studies of lima bean trypsin inhibitor
- Non-Boltzmann thermodynamic integration (NBTI) for macromolecular systems: Relative free energy of binding of trypsin to benzamidine and benzylamine
- Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: Qualitative evaluation of electrostatic differences at the substrate binding site
- Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b5 and the structural comparison with Val61His mutant
- Trypsin-induced follicular papilla apoptosis results in delayed hair growth and pigmentation
- Serum trypsinogen-2 and trypsin-2-α1-antitrypsin complex in malignant and benign digestive-tract diseases. Preferential elevation in patients with cholangiocarcinomas
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