9087-70-1
Trypsin inhibitor, pancreatic basic
CAS: 9087-70-1;9004-04-0
Molecular Formula: C284H432N84O78R2S7
9087-70-1 - Names and Identifiers
9087-70-1 - Physico-chemical Properties
| Molecular Formula | C284H432N84O78R2S7 |
| Molar Mass | 6495.43988 |
| Melting Point | >234oC (dec.) |
| Water Solubility | Freely soluble in water and in aqueous buffers of low ionic strength. |
| Solubility | Easily soluble in water, normal saline, insoluble in ethanol, acetone, ether. |
| Appearance | lyophilized powder |
| Color | white |
| Merck | 13,761 |
| Storage Condition | 2-8°C |
| Stability | Stable. Incompatible with strong oxidizing agents. |
| MDL | MFCD00162935 |
| Physical and Chemical Properties | White or beige dry powder. Easily soluble in water, normal saline, insoluble in ethanol, acetone, ether. |
| Use | Protease inhibitors for acute bleeding caused by various Fibrinolysis |
| In vitro study | Aprotinin is an antifibrinolytic small molecule that inhibits trypsin and related proteolytic enzymes. In cell biology, aprotinin is used as a protease inhibitor to prevent protein degradation when lysing, homogenizing tissues and cells. Aprotinin inhibits fibrinolytic activity in a dose-dependent manner with prolonged clotting time. In vitro, Aprotinin is a potent endogenous coagulation pathway inhibitor. |
| In vivo study | Aprotinin inhibits clot lysis in vitro, prolongs tail-cutting bleeding time in vitro in rats, and prolongs clotting time in human plasma. aprotinin reduces thrombus weight in a rat model of arteriovenous shorting. |
9087-70-1 - Risk and Safety
| Risk Codes | R42/43 - May cause sensitization by inhalation and skin contact. R36/37/38 - Irritating to eyes, respiratory system and skin. R20/21/22 - Harmful by inhalation, in contact with skin and if swallowed. |
| Safety Description | S22 - Do not breathe dust. S45 - In case of accident or if you feel unwell, seek medical advice immediately (show the label whenever possible.) S36/37 - Wear suitable protective clothing and gloves. S36 - Wear suitable protective clothing. S26 - In case of contact with eyes, rinse immediately with plenty of water and seek medical advice. |
| WGK Germany | 1 |
| RTECS | YN5080000 |
| FLUKA BRAND F CODES | 10-21 |
| HS Code | 35040000 |
| Toxicity | LD50 i.v. in mice: 2500000 kallikrein inhibitor units/kg (Trautschold) |
9087-70-1 - Reference
| Reference Show more | 1. Zhang Yifan, Wang Qiang, Wang Wei, etc. Study on the stability of antioxidant and hypoglycemic activity of Myrica rubra proteolytic peptides [J]. Science and Technology of Food Industry, 2015, 36(014):86-91. 2. LV Juan, Zhou Gang, Li Zhenlian, Du Yan, Zhu Yeqing. Determination of molecular weight distribution of polypeptides in peptone by gel filtration chromatography [J]. Journal of Food Safety and quality testing, 2020,11(15):5131-5136. 3. Jin Jian, Ma Haile, Qu Wenjuan, etc. Effect of ultrasonic pretreatment on enzymatic hydrolysis of corn protein [J]. Chinese Journal of cereal and oil, 2015, 30(11):58-64. 4. LV Juan, Zhou Gang, Li Zhenlian, Du Yan, Zhu Yeqing. Determination of molecular weight distribution of polypeptides in peptone by gel filtration chromatography [J]. Chinese Journal of Food Safety and quality testing, 2020,11(15):5131-5136. 5. Tan, Chunye, et al. "Expression of MicroRNA-29a regulated by yes-associated protein modules the neurite outgrowth in N2a cells." BioMed research international 2017 (2017).https://doi.org/10.1155/2017/5251236 6. [IF=5.118] Shan-Shan Zhang et al."Two Novel Multi-Functional Peptides from Meat and Visceral Mass of Marine Snail Neptunea arthritica cumingii and Their Activities In Vitro and In Vivo."Mar Drugs. 2018 Dec;16(12):473 7. [IF=7.514] Zhucheng Yin et al."Analysis of the interaction between cyanidin-3-O-glucoside and casein hydrolysates and its effect on the antioxidant ability of the complexes."Food Chem. 2021 Mar;340:127915 8. [IF=4.411] Yaru Wu et al."Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-O-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition."Molecules. 2021 Jan;26(6):1721 9. [IF=2.696] He Zhang et al."Transdermal permeation effect of collagen hydrolysates of deer sinew on mouse skin, ex vitro, and antioxidant activity, increased type I collagen secretion of percutaneous proteins in NIH/3T3 cells."J Cosmet Dermatol-Us. 2020 Feb;19(2):519 10. [IF=5.396] Hongdong Song et al."Digestion characteristics of quinoa barley and mungbean proteins and the effects of their simulated gastrointestinal digests on CCK secretion in enteroendocrine STC-1 cells."Food & Function. 2022 May;: 11. [IF=6.057] Supan Cheng et al."Liquid crystal-based sensitive and selective detection of uric acid and uricase in body fluids."Talanta. 2022 Jul;244:123455 |
9087-70-1 - Nature
Open Data Verified Data
The peptidase inhibitor of this strain was extracted and purified from bovine pancreas, bovine parotid gland and bovine lung. White or yellowish powder. Soluble in water or saline, insoluble in ethanol, acetone or ether. Odorless, dialyzable, isoelectric point of the pH value of 10~10.5. It is stable to high temperature, acid and alkali. In dilute acid heating to 100 deg C, pH12.6 at room temperature for 24h is still very stable, but in pH12.8 decreased viability. It can be digested by thermophilic protease at 60~80 ℃, and is more stable to other enzymes. It is not an enzyme itself, but a polypeptide, a broad-spectrum inhibitor of the enzyme. Containing 58 amino acids, the molecular weight of about 6500u. It can compete with the activity center of various proteases for a lysyl group and inhibit its activity. This product in vivo elimination is very fast, its plasma half-life of about 150min.
Last Update：2024-01-02 23:10:35
9087-70-1 - Preparation Method
Open Data Verified Data
can be extracted from the lungs of cattle, human urine, the main domestic extracted from the lungs of fresh cow lung washed clean, minced with meat grinder. Then add 5 times the volume of water, stirred evenly, with 2. 5mol/L sulfuric acid was adjusted to pH 2.0, stirred and extracted for 8H, and then filtered with double gauze. The filter residue was repeated and extracted once again, and the two extracts were combined. 277g per liter of ammonium sulfate was added to the extract, and the mixture was stirred, adjusted to pH 1.5 with 5mol/L of sulfuric acid, and allowed to stand overnight. The supernatant was taken up and filtered, and the pH of the filtrate was adjusted to 5.5. Ammonium sulfate was added to the filtrate by adding 255g per liter, and the mixture was homogenized and allowed to stand for 48 hours. The salting-out material was dissolved in 8-10 times of water, and allowed to stand overnight at 4 ℃. The precipitate was filtered off, and 50% trichloroacetic acid (1/20 of the filtrate) was added to the filtrate, rapidly heated to 80 ° C and then rapidly cooled to 30 ° C, filter to remove the precipitate, then adjust the pH to 20% with 610 sodium hydroxide, then add ammonium sulfate (grams per liter of filtrate), stir and dissolve, the mixture was allowed to stand overnight, and the salting-out material was collected. The salting-out substance is used 5 times more than 0.1 mol/L sodium acetate (pH 5.5) buffer solution and 1 volume of boric acid buffer solution were dissolved, and magnesium sulfate (plus 1050g per liter) was added. The solution was stirred and left to stand overnight, and the precipitate was collected and the filtrate was discarded. After dissolving the precipitate with 4 times the volume of water, dialysis 24h, and then diatomite filtration, filtrate with 201 × 7 and 001 × 7 type resin adsorption (the ratio of the two is 3:1), the resin was filtered to obtain a desalting solution. Desalting solution plus 0.9% sodium chloride and 1.5 times the precipitation of acetone, filtration. The precipitate was washed with acetone and ether, dried, redissolved in 80% methanol, and filtered. The filtrate was further added with an appropriate amount of sodium chloride and acetone, and the mixture was homogenized, allowed to stand overnight, centrifuged, and the precipitate was washed with acetone and dried to obtain a precipitate. The precipitate was dissolved in pyrogen-free water, adjusted to pH 11, left overnight at 4 °c, filtered, and the filtrate was adjusted to pH 4-5 with acetic acid, then 1% sodium chloride solution (concentration 30%) and 5 times the amount of acetone were added, and allowed to stand overnight. The precipitate was collected, washed with acetone and ether, and dried to obtain a finished product.
Last Update：2022-01-01 11:11:46
9087-70-1 - Standard
Authoritative Data Verified Data
This strain extracted and purified from bovine pancreas or bovine lung to obtain the polypeptide with the activity of inhibiting proteolytic enzyme. The activity of aprotinin should not be less than 3.0 units per 1 mg calculated as anhydrous.
Last Update：2024-01-02 23:10:35
9087-70-1 - Trait
Authoritative Data Verified Data
- This product is white to yellowish powder.
- This product is soluble in water or 0.9% sodium chloride solution, insoluble in ethanol, acetone or ether.
Last Update：2022-01-01 11:56:26
9087-70-1 - Application
Open Data Verified Data
- protease inhibitor. Inhibition of trypsin, indirect inhibition of chymotrypsin, elastase, carboxypeptidase and various tissues, blood kallikrein.
- usage and dosage in the treatment of acute pancreatitis, dosage of 100,000 KIU intravenous drip, 1~2 times a day; Inhibition of fibrinolytic enzyme activity, for the treatment and prevention of excessive dissolution of fibrin caused by bleeding and postpartum hemorrhage; Inhibition of kallikrein, for a variety of causes of Shock, in particular, it can also prevent and treat the formation of fat embolism after traumatic Shock, and prevent respiratory insufficiency after trauma. Intravenous injection of 500,000 KIU within 10 minutes for the first time, followed by additional injection of 200,000~300,000 KIU every 6 hours (within 6 minutes) for 48~96 hours, before the surgical incision was closed, 20,000~40,000 KIU was injected into the abdominal cavity at a time. For chronic Allergic urticaria and angioneurotic edema, the curative effect is remarkable, intravenous injection of 10 units/time, once every other day, a course of 15~20 times. It also has a unique therapeutic effect on skin disorders.
Last Update：2025-08-19 16:24:40
9087-70-1 - Legal requirements
Authoritative Data Verified Data
This product should be extracted from Quarantine qualified bovine pancreas or lung, and the production process should comply with the requirements of the current version of "good manufacturing practice.
Last Update：2022-01-01 11:56:26
9087-70-1 - Safety
Open Data Verified Data
- a small number of people have allergic reactions, erythema, urticaria, bronchospasm, should be discontinued. Intravenous injection of Too Slow even can cause Vomit, Nausea, Diarrhea, myalgia, blood pressure changes.
- under shading, sealed and preserved.
Last Update：2022-01-01 11:11:47
9087-70-1 - Differential diagnosis
Authoritative Data Verified Data
- (1) take this product and trypsin, add water separately to dissolve and dilute to make a solution containing lmg in each lml, take 10u1 and set it on a drop plate, mix it well, add 0.2 of p-Toluenesulfonyl-L-arginine methyl ester hydrochloride solution. After several minutes, it should not show purplish red color. To trypsin solution 10u1 as control, the same method of operation, should be purple red.
- (2) in the chromatogram recorded under N-pyroglutamyl-Aprotinin and related substances, the retention time of the main peak of the test solution should be consistent with the retention time of the main peak of the control solution.
Last Update：2022-01-01 11:56:27
9087-70-1 - Exam
Authoritative Data Verified Data
absorbance
take this product, precision weighing, adding water to dissolve and quantitatively dilute the solution containing 3.0 units per lml, according to UV-visible spectrophotometry (General 0401) determination, there is a maximum absorption at the wavelength of 277nm, the absorbance should not exceed 0.8.
acidity
take this product, add water to dissolve and dilute the solution containing 5mg per lml, and determine it according to law (General 0631). The pH value should be 5.0~7.0.
clarity of the solution
take this product, add water to dissolve and dilute the solution containing 2mg per lml, check according to law (General Principles 0902 first method), the solution should be clarified.
Off-molecular protein
take this product, add water to dissolve and dilute to make a solution containing 5 units per 1 ml as a test solution; Take the appropriate amount of aprotinin that has been heated at 112 ° C for 2 hours, water was added to dissolve and diluted to make a solution containing 5 units per 1 ml as a system-suitable solution. According to the determination of molecular exclusion chromatography (General rule 0514), hydrophilic modified silica gel is used as the filler (TSK-G4000SWxl column, 7.8 ×, 8um or other suitable column), and 3 columns are connected in series; the mobile phase was 3mol/L acetic acid solution, the flow rate was 1.0ml per minute, the detection wavelength was 280nm, and the column temperature was 35. Take the applicable solution 100 u1 of the system, inject human liquid chromatography, record the chromatogram, the retention time of dimer peak relative to aprotinin peak is about 0.9; The separation degree between dimer peak and aprotinin peak should be more than 1.0; the tailing factor of the main peak of aprotinin should not be greater than 2.5. Take Test Solution 100 u1, inject human liquid chromatograph, record chromatogram. Retention time is less than the main peak of aprotinin are high molecular protein peak, according to the peak area normalization method, the total amount of high molecular protein shall not be greater than 1.0%.
dealanine-deglycine-Aprotinin and dealanine-aprotinin
take an appropriate amount of this product, add water to dissolve and dilute to make a solution containing about 5 units per 1 ml, as a test solution; Take an aprotinin reference, water was added to dissolve and diluted to prepare a solution containing 5 units per 1 ml as a control solution. Capillary electrophoresis (
0542) determination, using fused silica capillary column (75umX 60cm, effective length 50cm); 120mmol/ L potassium dihydrogen phosphate buffer (pH 2.5) as the buffer solution; The detection wavelength was 214nm; the capillary temperature was 30°C; The operating voltage was 12kV. The migration time of dealanine-deglycine-aprotinin peak relative to aprotinin peak was 0.98, and the migration time of dealanine-aprotinin peak relative to aprotinin peak was 0.99; the degree of separation between the dealanine-deglycine-aprotinin peak and the dealanine-aprotinin peak should be greater than 0.8, and the degree of separation between the dealanine-aprotinin peak and the aprotinin peak should be greater than 0.5. The tailing factor of the aprotinin peak should not be greater than 3. The injection end was positive, and the sample was injected at a pressure of 1.5kPa, and the injection time was 3 seconds. Prior to each injection, the capillary column was washed with 0.1 mol/L sodium hydroxide solution, deionized water, and handling buffer for 2, 2, and 5 minutes in sequence. The electrophoresis spectrum of the test sample shall be calculated according to the formula of Lo (r1
2), where r1 is the corrected peak area (peak area/migration time) for dealanine-deglycine-Aprotinin or dealanine-aprotinin, r2 is dealanine-deglycine-aprotinin, sum of the corrected peak areas of dealanine-Aprotinin and aprotinin. The amount of dealanine-deglycine-aprotinin should not be greater than 8.0%, and the amount of dealanine-aprotinin should not be greater than 7.5%.
N-pyroglutamyl-Aprotinin and related substances
take an appropriate amount of this product, add mobile phase A to dissolve and dilute to make A solution containing 5 units per lml, as A test solution; Take an aprotinin reference, mobile phase A was added and dissolved and diluted to prepare A solution containing 5 units per 1 ml as A control solution. According to the high performance liquid chromatography (General 0512) determination, using the cation column (TSK-GEL IC-Cation-SW column, 7.8 mmX7.5cm,10um or other suitable column); Phosphate buffer solution (take potassium dihydrogen phosphate 3.52g, 7.26g disodium hydrogen phosphate, 3.52 ml water to dissolve) as mobile phase A, phosphate-ammonium sulfate buffer solution (7.26g of potassium dihydrogen phosphate, 66.07g of disodium hydrogen phosphate, g of ammonium sulfate, ml water to dissolve) mobile Phase B, gradient elution was carried out as follows; Flow rate was 1.0ml per minute; Detection wavelength was 210nm; Column temperature was 40°C. The retention time of aprotinin peak is about 17-20 minutes; The retention time of N-pyroglutamyl-aprotinin peak relative to aprotinin peak is 0.9; the degree of separation between the peak of N-pyroglutamyl-Aprotinin and the peak of aprotinin should be greater than 1.0; The tailing factor of the peak of aprotinin should be greater than 2.0. The sample solution 40 u1 was injected into the liquid chromatograph and the chromatogram was recorded. According to the peak area normalization method, the peak area of N-pyroglutamyl-aprotinin shall not be greater than 1.0%; The peak area of a single unknown impurity shall not be greater than 0.5%, and the sum of the peak areas of unknown impurities shall not be greater than 1.0%.
moisture
take this product, according to the moisture determination method (General 0832 first method 1), the water content shall not exceed 6.0%.
pyrogen
take this product, add Sterile Water for Injection to dissolve and dilute to make a solution containing 15 units per lml, check according to law (General rule 1142), and inject 1ml per lkg of rabbit body weight, the requirements shall be met.
abnormal toxicity
take this product, add sodium chloride injection to dissolve and dilute the solution containing 4 units per lml, check according to law (General rule 1141), should comply with the provisions.
antihypertensive substances
take this product, and add the gas of sodium injection solution and dilution, according to the law to check (General 1145), the dose of cat weight per lkg injection 1.5 units, should meet the requirements.
Last Update：2022-01-01 11:56:28
9087-70-1 - Titer determination
Authoritative Data Verified Data
preparation of substrate solution
benzoyl-L-Arginine ethyl ester hydrochloride (171.3mg) was dissolved in water and diluted to 25ml. New system was applied.
preparation of trypsin solution
take an appropriate amount of trypsin reference substance, weigh it accurately, add hydrochloric acid titration solution (0.001mol/L) to dissolve and quantitatively dilute it into about 0.8 units per lml (about 1 mg per lml) the solution, immediately with the new system and put the ice bath.
preparation of trypsin diluent
1ml of the trypsin solution was accurately weighed, placed in a 20ml measuring flask, diluted to the mark with a borax-calcium chloride buffer solution (pH 8.0), shaken, and placed in an ice bath for 10 minutes.
preparation of test solution
take an appropriate amount of this product, precision weighing, plus borax-calcium chloride buffer (pH 8.0) dissolved and quantitatively diluted to make about 1.67 units per lml (about 0.6mg per lml) take 0.5ml of the solution and 2ml of trypsin solution, put it in a 20ml measuring flask, dilute it to the scale with borax-calcium chloride buffer (pH 8.0), shake well, and react for 10 minutes, place in an ice bath (use within 2 hours).
assay
borax-calcium chloride buffer (pH 8.0)9.0 ML and substrate solution 1.0 ML, put in a 25ml beaker, place in a constant temperature water bath at 25°C ± 0.5°C for 3-5 minutes, and add sodium hydroxide titration solution (0.1 mol/U adjust the pH value to 8.0, add 1 ml of human test solution (incubated at 25 ° C. For 3-5 minutes), and immediately time, with a 1 ml micro Burette with sodium hydroxide titration solution (O. 1 mol/L) titrated the liberated acid to maintain the pH of the solution at 7.9-8.1 throughout. The volume (ml) of the sodium hydroxide titration solution (8.0 mol/L) consumed at a pH value of was read every 60 seconds for 6 minutes. In addition, 1 ml of the trypsin dilution was accurately taken, and the above method was used as a control (repeated once). The time is plotted on the abscissa and the consumed sodium hydroxide titration solution (0.lmol/L) is plotted on the ordinate and should be a straight line. The two straight lines for the test and the control should be basically coincident, and the volume (ml) of sodium hydroxide titration solution (0.1 mol/L) consumed per second should be calculated.
titer unit definition
inhibits one trypsin unit [one trypsin unit per second for N-benzoyl-L-Arginine ethyl ester (BAEE) capable of hydrolyzing lumol] the activity is called an aprotinin activity Unit (EPU). Aprotinin is equivalent to 1800Kiu per 1EPU.
aprotinin activity
is an assay for inhibition of trypsin of known activity. The difference between the original activity and the residual activity of trypsin was used to calculate the units of activity.
Last Update：2022-01-01 11:56:29
9087-70-1 - Category
Authoritative Data Verified Data
protease inhibitors.
Last Update：2022-01-01 11:56:29
9087-70-1 - Storage
Authoritative Data Verified Data
under shading, sealed and preserved.
Last Update：2022-01-01 11:56:29
9087-70-1 - Aprotinin for injection
Authoritative Data Verified Data
This product is a sterile lyophilized product of aprotinin. The titers containing aprotinin should be between 85.0% and 120.0% of the labeled amount.
trait
This product is white or off-white lyophilized cake or powder.
identification
- This product is dissolved in water and diluted to prepare a solution containing 3 units per 1 ml as a test solution. The same results were shown in the identification (1) Test under aprotinin.
- in the chromatogram recorded under N-pyroglutamyl-Aprotinin and related substances, the retention time of the main peak of the test solution should be consistent with the retention time of the main peak of the control solution.
examination
- acidity take this product, add 2ml of water to dissolve, and then determine according to law (General 0631),pH value should be 5.0~7.03
- the color of the solution is taken from this product, dissolved with water and diluted to prepare a solution containing 6 units per lml, which should be colorless; If the color is developed, comparison with yellow No. 2 Standard Colorimetric solution (General rule 0901 first method), not deeper.
- high molecular protein take this product, according to the method under the item of aprotinin, the total amount of high molecular protein should not be greater than 1.5%.
- the moisture content of this product shall not exceed 0832 as determined by the method for determination of moisture (General rule 7.0%, first method 1).
- allergic reaction take an appropriate amount of this product, add sodium chloride injection to dissolve and dilute to prepare a solution containing 0.065 units per lml, and check according to law (General rule 1147).
- dealanine-deglycine-Aprotinin and dealanine-aprotinin, N-pyroglutamyl-Aprotinin and related substances, Pyrogen and hypotensive substances were examined according to the method under aprotinin, all shall be in accordance with the provisions.
- others should comply with the relevant provisions under injection (General 0102).
titer determination
take 5 pieces of this product, respectively, precision plus borax-calcium chloride buffer (PH8.0)2ml dissolved and combined, mixed. Take an appropriate amount (about 33.4 units containing aprotinin), put it in a 20ml measuring flask, dilute it to the scale with borax-calcium chloride buffer (pH 8.0), and shake it well, take 0.5ml and 2ml of trypsin solution, put them in a 20ml measuring flask, dilute to the mark with borax-calcium chloride buffer (pH 8.0), shake well, and react for 10 minutes, immediately measured and calculated according to the method under aprotinin.
category
Same as aprotinin.
specification
- 28 units (50,000 KIU)
- 56 units (100,000 KIU)
- 112 units (200,000 KIU)
- 278 units (500,000 KIU)
storage
shade, close, and store in a cool place.
Last Update：2022-01-01 11:56:30
9087-70-1 - Trait
White or off-white dry powder.
Last Update：2023-08-16 21:32:38
9087-70-1 - Vitality definition
1 U corresponds to 1 biological kallikrein inhibitor unit (KIU)
Last Update：2023-08-16 21:32:38
9087-70-1 - Loss on drying
≤6.0%
Last Update：2023-08-16 21:32:38
9087-70-1 - Reference Information
| biological activity | Aprotinin is an inhibitor of serine protease (Kd value for bovine β-trypsin is 0.06 pM), which is used to reduce perioperative blood loss and blood transfusion. |
| target | TargetValue Thrombin (Cell-free Trypsin) 0.06 pM(Kd) kallikrein (Cell-free assessment) 0.8 nM(Kd) chymotrypsin (Cell-free assessment) 9.5 nM(Kd) trypsinogen (Cell-free assessment) 2 μM(Kd) |
| Value | |
| Thrombin (Cell-free assay) | |
| Trypsin (Cell-free assay) | 0.06 pM(Kd) |
| kallikrein (Cell-free assay) | 0.8 nM(Kd) |
| chymotrypsin (Cell-free assay) | 9.5 nM(Kd) |
| trypsinogen (Cell-free assay) | 2 μM(Kd) |
| in vitro study | Aprotinin is an anti-fibrinolytic small molecule that inhibits trypsin and related proteolytic enzymes. In cell biology, aprotinin are used as protease inhibitors to prevent protein degradation when cleaving and homogenizing tissues and cells. Aprotinin inhibited fibrinolytic activity in a dose-dependent manner with prolonged coagulation time. In vitro, Aprotinin is an effective endogenous coagulation pathway inhibitor. |
| in vivo study | Aprotinin inhibit blood clot dissolution in vitro, prolong the bleeding time of rat tail cutting in vitro, and prolong the coagulation time in human plasma. In the rat arteriovenous short circuit model, aprotinin can reduce thrombus weight. |
| chemical properties | white or beige dry powder. Easily soluble in water, normal saline, insoluble in ethanol, acetone, ether. |
| use | peptidase inhibitor. It can inhibit trypsin, chymotrypsin and fibrinolytic enzyme. Used for fibrinolysis, acute pancreatitis and pancreatic necrosis. |
| production method | fresh or frozen beef lung is minced, extracted with water, and salted out with ammonium sulfate. Salted out with trichloroacetic acid to remove protein, and then through dialysis, desalting, precipitation and other multi-step operations to obtain aprotinin. The total yield is about 23%. |
| toxic substance data | information provided by: pubchem.ncbi.nlm.nih.gov provided (external link) |
Last Update：2024-04-09 21:48:26
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