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 English: Trypsin activity: 10000U/gCAS :9002-07-7. 
 As a protease, EC3.4.21.4. In vertebrates, as the digestive enzymes which play a role. Enzymes in the pancreas as trypsinogen precursors were synthesized. As a component of pancreatic juice and secretion by the enterokinase, restriction or trypsin-activated decomposition into trypsin, the peptide chain enzyme, it can polypeptide chain of lysine and arginine residues in the carboxyl side of the cut. It not only played the role of digestive enzymes, but also to limit decomposition of the original chymotrypsin, carboxypeptidase zymogen, plasminogen, and other enzymes of phospholipid precursors, since activation. Is the most specific protease, in determining the protein's amino acid sequence, it became an indispensable tool. 
 Introduction 
 Bovine trypsin 223 amino acid residues, molecular weight of 23300, the active site serine residue is essential serine protease. In addition to exist in vertebrates, but also present in the silkworm, starfish, La Regardless, actinomycetes bacteria in a wide range of organisms. Also with the higher animals such as blood coagulation and inflammation related to thrombin, plasmin, vasodilator factors such as protease in chemical structure and specificity of trypsin and other aspects of a close relationship that these enzymes are enzymes from a common ancestor differentiation in the evolutionary process from the. Chymotrypsin and pancreatic elastase in the structure and catalytic mechanism is also a close relationship, but its specificity is quite different. 
 Department of trypsin from cattle, sheep or pig pancreatic extract a proteolytic enzyme. Standards for Chinese medicines by drying product terms, each not less than 1mg potency of 2500 units. By the cattle, sheep, pig pancreas extract derived from a peptide chain enzymes, only lysine or arginine carboxyl fracture in the formation of the peptide bond. White or yellow crystalline powder. Soluble in water, molecular weight 24 000, pI 10.5, the optimum pH of about 7.8 to 8.5. pH> 9.0 irreversible inactivation. Ca2 + have a stabilizing effect on enzyme activity; heavy metal ions, organic phosphorus compounds, DFP, natural trypsin inhibitors strongly inhibited its activity. Clinical use of anti-inflammatory swelling, industry for the manufacture of leather, silk processing, food processing and so on. 
 Function and use 
 Product of protein enzymes, proteins can be selectively hydrolyzed by lysine or arginine carboxyl peptide posed, can digest dissolved in denatured egg quality, undenatured protein of no effect, therefore, make the pus, sputum, blood clots and other decomposition, thinning and easy drainage of exclusion, accelerated wound clean and promote new granulation tissue, in addition to anti-inflammatory effect. Clinic for empyema, hemothorax, surgical inflammation, ulcers, traumatic injury, fistula, etc. produced by local edema, hematoma, and abscess. Aerosol inhalation for respiratory diseases. Can also be used to treat snake bites. Also commonly used in animal cell culture of the organization before the treatment.