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Trypsin in clinical research

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

Trypsin in clinical research

A brief introduction to trypsin

Trypsin is an enzyme. Work in the small intestine, it will hydrolyze the protein peptide, and then broken down into amino acids. This is the necessary process for protein to be absorbed by the body. The principle of this enzyme and other serine protease almost.

Overview of trypsin

Bovine trypsin amino acid residues 223, molecular weight 23800, the active site of the serine residue is indispensable serine protease. In addition to the presence of vertebrates, but also in the silkworm, sea plate car, the United States, actinomycetes and other wide range of organisms. In addition, the proteases such as thrombin, plasmin, and vasopressin, which are related to blood coagulation and inflammation of higher animals, are closely related to trypsin in terms of chemical structure and specificity. It is believed that these enzymes are derived from common ancestral enzymes In the evolution of the process of differentiation. Pancreatic trypsin and elastase are also closely related to structural and catalytic mechanisms, but their specificity is completely different.

Trypsin is a proteolytic enzyme extracted from cattle, sheep or pig pancreas. Chinese pharmaceutical standards for dry products, the price per 1mg shall not be less than 2500 units. A peptide endonuclease derived from cattle, sheep, and porcine pancreas is involved only in the formation of peptide bonds in which the carboxyl groups of lysine or arginine are involved. White or beige crystalline powder. Soluble in water, insoluble in ethanol, glycerol, chloroform and ether. Molecular weight 24 000, pI 10.5, the optimum pH value of 7.8 to 8.5 or so. PH> 9.0 irreversible inactivation. Ca2 + has a stabilizing effect on the enzyme activity; heavy metal ions, organophosphorus compounds, DFP, natural trypsin inhibitors have a strong inhibitory activity. Clinical for anti-inflammatory swelling, industrial for leather manufacturing, raw silk processing, food processing.

Pharmacology and Toxicology of Trypsin

Trypsin with the role of endopeptidase, selectively acting on denatured proteins to hydrolyze into peptides or amino acids, improve tissue permeability, inhibit edema and thrombosis around the inflammatory reaction; dissolved blood clots, exudate, necrosis Organization; decomposition of sputum, pus and other viscous secretions; to promote the rapid diffusion of local liquid absorption.

The role and use of trypsin

Trypsin for protein hydrolase, can selectively hydrolyze the protein from the lysine or arginine carboxyl group formed by the peptide chain, can digest and dissolve denatured egg, the non-denatured protein no effect, therefore, can make pus, Sputum, blood clot and other decomposition, thinning, easy to exclude drainage, accelerate the wound purification, promote granulation tissue newborn, in addition to anti-inflammatory effect.

Trypsin is used clinically for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula and other local edema, hematoma and abscess. Spray inhalation for respiratory diseases. Can also be used to treat snake bites. Also used for animal cell culture before the treatment of tissue.

The dosage and usage of trypsin

Trypsin is mainly through intramuscular injection, 1 000 ~ 2 000U or 5 000U with saline or water for injection, 1 times / day. Snake bites, take this product 2 000U, 1 to 3, plus 0.25% to 0.5% procaine hydrochloride solution (or water for injection) 4ml ~ 20ml dissolved to the tooth marks as the center, around the wound infiltration injection The Or in the swelling of the top of the ring closed for 1 or 2 times, such as the need to reusable.

Use of trypsin precautions

Trypsin can not be used for acute inflammation, hemorrhagic cavity, pulmonary hemorrhage within a week. Liver, renal insufficiency, hemagglutination mechanism abnormalities and bleeding patients disabled.

Medication with a needle before dipping this product for skin scratches test. Showing a negative reaction before injection. This product is unstable in aqueous solution, dissolved after the rapid decline in the price, it should be prepared before the solution.

Trypsin side effects

1. injection of local pain, induration.

2. Trypsin can cause histamine release, resulting in systemic reactions, chills, fever, headache, dizziness, chest pain, abdominal pain, rash, angioneurotic edema, dyspnea, increased intraocular pressure, leukopenia. Symptoms of light does not affect the continued treatment, given antihistamines and symptomatic drugs can be controlled, severe should be discontinued.

3. This product can cause allergic shock.

Cell culture of trypsin

The role of trypsin is to make the cells between the protein hydrolysis and thus the cells scattered. Different tissues or cells respond differently to trypsin. The activity of trypsin-dispersed cells is also related to its concentration, temperature and time of action. At pH 8.0 and the temperature is 37℃, the activity of trypsin solution is the strongest. When using trypsin, you should grasp the concentration, temperature and time, so as not to cause excessive cell damage. Because of Ca2+, Mg2+ and serum, protein can reduce the activity of trypsin, so the preparation of trypsin solution should be used without Ca2+, Mg2+ BSS, such as: D-Hanks solution. Termination of digestion, can be used to contain serum or trypsin inhibitor to stop the role of trypsin on cells.

1. Weigh trypsin: trypsin solution concentration of 0.25%, with an electronic balance accurately weighed into a small beaker in the double distilled water (if the need for double distilled water to adjust to 7.2 or so) or PBS (D-Hanks. Stir well and mix overnight at 4 °C.

2. with the filter filter sterilization: with a good tryptic solution in the clean bench with a filter (0.22 micron microporous membrane) filter sterilization.

3. Packed into vials stored at -20 ℃ for use!

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