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 |
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 |
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.
This product is white or off-white crystalline powder.
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.
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.
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.
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.
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).
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.
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.
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.
proteolytic enzymes.
shade, seal, and store in a cool and dry place.
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.
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.
This product is white or off-white lyophilized cake or powder.
take about 5000 units of this product and show the same reaction according to the identification test under trypsin.
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.
Same as trypsin.
(1) 12,500 units (2) 25,000 units (3) 50,000 units (4) 100,000 units
sealed and kept in a cool dark place.
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) |