Trypsevas
trypsin
CAS: 9002-07-7;2594-14-1
Molecular Formula: C35H47N7O10
Trypsevas - Names and Identifiers
Trypsevas - Physico-chemical Properties
| Molecular Formula | C35H47N7O10 |
| Molar Mass | 725.78858 |
| Density | 1.37[at 20℃] |
| Melting Point | 115°C |
| Water Solubility | Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml). |
| Solubility | Reconstitute in aqueous buffer |
| Vapor Presure | 0Pa at 25℃ |
| Appearance | lyophilized powder |
| Color | White powder |
| Odor | Odorless |
| Merck | 13,9865 |
| pKa | pK1:6.25 (25°C,μ=0.1) |
| Storage Condition | -20°C |
| Stability | Stable. Incompatible with strong oxidizing agents. |
| MDL | MFCD00082094 |
| Physical and Chemical Properties | Melting Point: 115°C |
| Use | Used for various surgical ulcers and inflammatory gangrene, wound azole injury, fistula hole and other edema, worm |
Trypsevas - Risk and Safety
| Risk Codes | R36/37/38 - Irritating to eyes, respiratory system and skin. R42 - May cause sensitization by inhalation R42/43 - May cause sensitization by inhalation and skin contact. |
| Safety Description | S22 - Do not breathe dust. S24 - Avoid contact with skin. S26 - In case of contact with eyes, rinse immediately with plenty of water and seek medical advice. S36/37 - Wear suitable protective clothing and gloves. S45 - In case of accident or if you feel unwell, seek medical advice immediately (show the label whenever possible.) S23 - Do not breathe vapour. |
| WGK Germany | 2 |
| RTECS | GC3050000 |
| FLUKA BRAND F CODES | 1-3-10 |
| TSCA | Yes |
| HS Code | 35079090 |
Trypsevas - Nature
Open Data Verified Data
- The proteolytic enzyme extracted from bovine, ovine or porcine pancreas of this strain is white or off-white crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. It is stable at room temperature on drying. At a pH of 1.8, short boiling is hardly inactivated. The aqueous solution lost 75% of efficacy at room temperature for 3H. The aqueous solution is unstable at pH 6 and quite stable at pH 2~3. The protein precipitates with the addition of salt in the hot solution and the filtrate shows no enzymatic action. Caz + has protective and activating effects. Isoelectric point pl = 10.1.
- bovine trypsinogen consists of 229 amino acid residues, containing 6 pairs of disulfide bonds. The peptide bond between the N-terminal lysine and the isoleucine residue of the zymogen is hydrolyzed under the catalysis of enterokinase or autocatalysis, and the peptide "day" day "day" day "Lai 6 is released, became active trypsin, molecular weight 24000, is a single peptide chain consisting of 223 amino acid residues. Porcine trypsin is more stable than trypsin, and the unit is higher than that of cattle. Its isoelectric point pl = 10.8.
- trypsin acts exclusively on a peptide bond composed of the basic amino acids arginine and leucine carboxyl. The enzyme itself is very easy to dissolve, by the original B trypsin into a-trypsin, and then further degradation of trypsin and even fragments, the vitality is gradually decreased and lost. Since serum contains non-specific trypsin inhibitors, trypsin does not digest normal tissues. It can improve tissue permeability, strongly inhibit experimental edema, inhibit inflammation around the thrombus; Can quickly dissolve blood clots, exudate and necrotic tissue; Intravenous injection can prolong clotting time, but large doses instead promote blood coagulation, and even cause heart disorders; Decomposition of sputum, pus and other viscous secretions; Can promote the penetration of antibiotics, chemotherapy and other drugs to the lesion; A significant solution of snake venom.
Last Update：2024-01-02 23:10:35
Trypsevas - Preparation Method
Open Data Verified Data
- extraction method using bovine pancreas as raw material.
- extraction method using sheep pancreas as raw material.
- extraction method using porcine pancreas as raw material.
- after the pig pancreas was washed and cleaned, it was minced, and an aqueous acetic acid solution having a pH of 4 was added thereto. The mixture was stirred and extracted at 4 ° C. Or lower for 24 hours, followed by filtration. Ammonium sulfate was added to the filtrate to bring the concentration to 75% of saturation, and the mixture was centrifuged to obtain a salting-out precipitate. The supernatant was then salted out and precipitated [(NH4)2 S04 85% saturation], and separated by adsorption, and ribonuclease A was produced. 90g of the salting out precipitate was dissolved in 1L of distilled water, then 30g of CaCl2 powder was added, and the pH was adjusted to 8, then 5mg of crystalline trypsin was added, activated at 4 °c for 24h, filtered, filter off the precipitate and adjust the pH to 7.8, add p-aminobenzamidine-Sepharose 6B resin for Batch adsorption, then use 2 times the resin volume of pH 7.8 buffer (containing CaCl2,0.1 mol/L) washing, then loading column, and then formic acid (0.1 mol/L) -KCl(0.05 mol/L), pH 2.2 buffer solution elution, activity peak collection, dialysis, freeze drying, available trypsin.
Last Update：2022-01-01 11:10:49
Trypsevas - Standard
Authoritative Data Verified Data
proteolytic enzymes extracted from pig, sheep or bovine pancreas in this line. Calculated on a dry basis, trypsin activity per 1 mg should not be less than 2500 units.
Last Update：2024-01-02 23:10:35
Trypsevas - Trait
Authoritative Data Verified Data
This product is white or off-white crystalline powder.
Last Update：2022-01-01 15:38:07
Trypsevas - Application
Open Data Verified Data
- proteolytic enzyme. Surgery for a variety of inflammation, ulcers, gangrene, trauma, fistula hole caused by local abscess, edema, hematoma, but also for snake bites and other diseases. Dermatology is used to treat ringworm and other skin disorders. Internal medicine for empyema, emphysema, bronchitis, bronchial asthma and other diseases. It is also used in chemical industry, light industry, textile and other industries.
- usage and dosage before use, add appropriate amount of sodium chloride injection to dissolve. Intramuscular injection: Local injection or spray inhalation, the amount of the disease depending on the decision.
Last Update：2025-08-19 16:24:40
Trypsevas - Differential diagnosis
Authoritative Data Verified Data
take about 2mg of this product, put it on a white drip plate, add 0.2 of p-Toluenesulfonyl-L-arginine methyl ester hydrochloride test solution, stir well, then appear purple.
Last Update：2022-01-01 15:38:10
Trypsevas - Safety
Open Data Verified Data
- pain at the site of intramuscular injection, with induration, chills, Fever, Head Pain, chest pain, Abdominal Pain, Dyspnea, rash, angioedema, elevated intraocular pressure, leukopenia and other adverse reactions, but does not affect the drug; Generally given antihistamines and antidotes can be controlled; Rare allergic shock; Tuberculous empyema, tracheal pleural fistula in patients with caution. Can not be used for acute inflammation, bleeding cavity, pulmonary hemorrhage within one week; Liver, kidney injury, blood coagulation dysfunction and bleeding in patients with no use.
- light-shielding, closed, stored in a cool and dry place.
Last Update：2022-01-01 11:10:50
Trypsevas - Exam
Authoritative Data Verified Data
acidity
take this product, add water to dissolve and dilute the solution containing 2mg per lml, according to the law (General 0631),pH value should be 5.0~7.0.
clarity of the solution
take this product, add 0.9% sodium chloride solution to dissolve and dilute the solution containing lOmg per lml, check according to law (General Principles 0902 first method), the solution should be clarified.
chymotrypsin
preparation of substrate solution N-acetyl-L-tyrosine ethyl ester 23.7mg was placed in a volumetric flask, add phosphate buffer (0.067mol/L potassium dihydrogen phosphate solution 38.9ml and 0.067mol/L disodium hydrogen phosphate solution 61.1ml, mixed, pH 7.0)50ml, warm to dissolve, after cooling, dilute to the scale and shake. Frozen storage, but not repeated freeze-thaw. Preparation of Test Solution take appropriate amount of this product, precision weighing, add 0.OOlmol/L hydrochloric acid solution to dissolve and quantitatively dilute to prepare a solution containing 0.25mg per 1 ml.
2.0ml of the substrate solution and 7.0 M L of a 0. O01 mol/l hydrochloric acid solution were mixed with 1 ml of the above phosphate buffer (pH) to prepare a blank. Take 0.2ml of the test solution accurately, add 0.5 ml of the substrate solution (preheated to 25°C ± 3.0°C), immediately Time and shake, keep the temperature in the cuvette at 25°C ± 0.5°C and read the absorbance at a wavelength of 237nm every 30 seconds for 5 minutes by UV-Vis spectrophotometry (General 0401 ) , the rate of change of absorbance should be constant every 30 seconds, and the constant time should not be less than 3 minutes.
loss on drying
take an appropriate amount of this product, take phosphorus pentoxide as desiccant, and dry under reduced pressure at 60°C for 4 hours. The weight loss shall not exceed 5.0% (General rule 0831).
Last Update：2022-01-01 15:38:12
Trypsevas - Titer determination
Authoritative Data Verified Data
preparation of substrate solution
take N-benzoyl-L-Arginine ethyl ester hydrochloride 85.7mg, add water to make 100ml, as a substrate stock solution; Take 10ml, dilute with phosphate buffer (0.067mol/L potassium dihydrogen phosphate solution 13ml mixed with 0.067mol/L disodium hydrogen phosphate solution 87ML, pH 7.6) to ML, according to UV-visible spectrophotometry (General rule 0401), constant temperature at 25.0°C ± 0.5°C, with water as blank, absorbance was measured at the wavelength of 253nm, if necessary, the substrate solution can be used by adjusting the above substrate stock solution or phosphate buffer so that the absorbance is between 0.575 and 0.585. Should be used within 2 hours after preparation.
preparation of test solution
precision weigh the appropriate amount of this product, add 0.001mol/L hydrochloric acid solution to dissolve and quantitatively dilute to make a solution containing 50 to 60 trypsin units per 1 ml.
assay
3.0 of the substrate solution was collected, and 200 u1 of a 0. O01 mol/L hydrochloric acid solution was added thereto, and the mixture was mixed uniformly to prepare a blank. Another precision sample 200ul solution, plus substrate solution (constant temperature at 25.0°C ± 0.5°C)3.0, immediately timing, mixing, the temperature in the cuvette was maintained at 25.0 ° C. ± 0.5 ° C., and the absorbance was read at a wavelength of 0401 NM every 30 seconds for 5 minutes by UV-visible spectrophotometry (general). The absorbance is plotted on the ordinate and the time is plotted on the abscissa; The change of absorbance should be constant between 0.015 and 0.018 every 30 seconds, and the time in a linear relationship should not be less than 3 minutes.
Last Update：2022-01-01 15:38:14
Trypsevas - Category
Authoritative Data Verified Data
proteolytic enzymes.
Last Update：2022-01-01 15:38:14
Trypsevas - Storage
Authoritative Data Verified Data
shade, seal, and store in a cool and dry place.
Last Update：2022-01-01 15:38:14
Trypsevas - Legal requirements
Authoritative Data Verified Data
This product should be extracted from Quarantine qualified cattle, sheep or pig pancreas, the species of animals used should be clear, the production process should comply with the current version of the "good manufacturing practice" requirements.
Last Update：2022-01-01 15:38:15
Trypsevas - Trypsin for injection
Authoritative Data Verified Data
This product is a sterile lyophilized product of trypsin. Trypsin-containing viability units should be between 90.0% and 120.0% of the labeled amount.
trait
This product is white or off-white lyophilized cake or powder.
identification
take about 5000 units of this product and show the same reaction according to the identification test under trypsin.
examination
- acidity take this product, add water to dissolve and dilute to make a solution containing 5000 units per lml, and determine it according to law (General 0631). The pH value should be 5.0~7.0.
- the color of the solution is taken from this product, and 0.9% sodium chloride solution is added to dissolve and dilute to make a solution containing 25,000 units per 1 ml, which should be colorless; If color development occurs, comparison with yellow No. 2 Standard Colorimetric solution (General rule 0901 first method), not deeper.
- loss on drying: take about 0.2g of this product, use phosphorus pentoxide as desiccant, and dry under reduced pressure at 60°C for 4 hours. The loss of weight shall not exceed 8.0% (General rule 0831).
- abnormal toxicity take this product, add Sterile Water for Injection dissolved and diluted into 125 units per lml of solution, according to law inspection (General 1141), should comply with the provisions.
- sterile take this product, after dissolving with appropriate solvent, the membrane filtration method, according to the law inspection (General 1101), should comply with the provisions.
- others should comply with the relevant provisions under injection (General 0102).
titer determination
take 5 pieces of this product, add appropriate amount of 0.001mol/L hydrochloric acid solution to dissolve, and transfer the whole amount to the same 100ml measuring flask, dilute to the scale with the above hydrochloric acid solution, shake, an appropriate amount was accurately measured and quantitatively diluted with the above hydrochloric acid solution to prepare a solution containing about 50 to 60 units per 1 ml. The assay was performed according to the method under trypsin.
category
Same as trypsin.
specification
(1) 12,500 units (2) 25,000 units (3) 50,000 units (4) 100,000 units
storage
sealed and kept in a cool dark place.
Last Update：2022-01-01 15:38:15
Trypsevas - Trait
White or off-white powder.
Last Update：2023-08-16 21:32:38
Trypsevas - Source
Bovine pancreas.
Last Update：2023-08-16 21:32:38
Trypsevas - Loss on drying
≤5.0%。
Last Update：2023-08-16 21:32:38
Trypsevas - Reference Information
| LogP | -1.3 at 20℃ |
| EPA chemical substance information | information provided by: ofmpeb.epa.gov (external link) |
| Introduction | trypsin is a protease, EC 3.4.21.4. In vertebrates, it is characterized as a digestive enzyme. In the pancreas is synthesized as the precursor of the enzyme, trypsinogen. Secreted as a component of pancreatic juice, restricted by enterokinase, or trypsin, is broken down into activated trypsin, an endopeptidase that cleaves the carboxyl side of lysine and arginine residues in the polypeptide chain. It is not only the characteristics of digestive enzymes, but also can limit the decomposition of chymotrypsinogen, carboxypeptidase, phospholipase and other enzyme precursors, activation characteristics. Is the most specific protease, in determining the amino acid arrangement of the protein, it becomes an indispensable tool. |
| physiological action | trypsin belongs to the class of serine proteases, which can specifically act on the carboxy terminus of Lys or Arg residues of the peptide chain. It is involved in the important processes of metabolism, digestion, coagulation and other functions in the animal body. In the field of cell biology, trypsin can degrade the protein at the junction of the cell membrane and the culture dish, so that the two can be separated. In addition, since the tension of the cytoskeleton inside the cell itself and the surface tension of the culture solution become spherical, cell digestion is realized. |
| toxicity | ADI is not restrictive (FAO/WHO,2001). |
| uses | for biochemical studies, protein structure analysis and sequence studies, protein digestion and decomposition, commonly used in clinical treatment of various inflammation, ulcers, wounds, hematoma, edema, ringworm and other skin diseases, can also be used for the treatment of emphysema, bronchitis and other diseases. used for various surgical ulcers and inflammatory gangrene, wound oxazole injury, fistula and other edema, worm swelling trypsin can be used as a proteolytic enzyme. Surgery mainly with a variety of ulcers, inflammation, trauma, gangrene, fistula caused by local abscess, edema, but also for snake bites and other diseases; Dermatology is mainly used to treat ringworm and other skin diseases. Internal medicine is mainly used for empyema, emphysema, bronchitis, bronchial asthma and other diseases. But after the drug may cause chills, Fever, Head Pain, chest pain, Abdominal Pain, Dyspnea, rash, angioedema, elevated intraocular pressure, leukopenia and other adverse reactions, rare anaphylactic shock. The intramuscular injection site is prone to pain and induration. Can not be used for bleeding cavity, acute inflammation, pulmonary hemorrhage within a week of the patient disabled. Tuberculous empyema, tracheal pleural fistula in patients with caution. Liver, kidney injury, blood coagulation dysfunction and bleeding in patients with non-use. Before use, add sodium chloride injection appropriate amount to dissolve. Intramuscular injection: Local injection or spray inhalation, the amount of the disease depending on the decision. enzyme preparation. Mainly used for baking, meat tenderness, protein hydrolysis. biochemical study. White or off-white frozen dry powder or crystals. Is a pancreatic serine protease. Soluble in water, insoluble in organic solvents. Structural analysis and sequence study of proteins, digestion and decomposition of proteins. recombinant trypsin has the same enzymatic properties as animal-derived trypsin. It can be used instead of trypsin, and has many advantages, such as no impurity activity, high stability, no self-cutting, high activity; In use, no non-specific enzyme slice segment and self-slice segment appear. It is used for specific protein enzymolysis, protein sequencing, peptide mapping, proteomics research, Pancreatin digestion of peptides on Z-D gel, etc. |
| production method | was obtained by pancreas extraction from pig or cow. using bovine pancreas as raw material, trypsinogen was first prepared, activated and then precipitated by ammonium sulfate, then recrystallized and dialyzed. |
| toxic substance data | information provided by: pubchem.ncbi.nlm.nih.gov (external link) |
Last Update：2024-04-09 21:01:54
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