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Trypsin is a type of protease, EC 3.4.21.4. characterized in vertebrates as a digestive enzyme. It is synthesized in the pancreas as the enzyme precursor trypsinogen.
It is secreted as a component of pancreatic juice and is subject to restriction by enterokinase, or trypsin, to become activated trypsin, a peptide chain endonuclease that cuts off the carboxyl side of lysine and arginine residues in polypeptide chains.
It not only acts as a digestive enzyme, but also restricts the decomposition of the precursors of other enzymes such as chymotrypsinogen, carboxypeptidyl peptidyl peptidaseogen, phospholipaseogen, and other enzymes, and acts as an activating feature. It is the most specific protease, and it becomes an indispensable tool in determining the amino acid arrangement of proteins.
Uses of Trypsin.
Trypsin can be used as proteolytic enzyme. Surgery is mainly used for various ulcers, inflammation, trauma, gangrene, fistula caused by local abscess, edema, also used for venomous snake bites and other diseases; dermatology is mainly used for the treatment of scabies and other skin diseases.
Internal medicine is mainly used for abscess, emphysema, bronchitis, bronchial wheezing and other diseases. It is also used in the treatment of abscess, pulmonary emphysema, bronchitis and bronchial asthma. However, the drug may cause chills, fever, headache, chest pain, abdominal pain, dyspnea, rash, angioneurotic edema, increased intraocular pressure, leukopenia and other adverse reactions, rare anaphylactic shock.
The site of intramuscular injection is prone to cause pain and hardness. Not to be used in hemorrhagic cavities, acute inflammation, pulmonary hemorrhage within a week of the patient is prohibited. Use with caution in patients with tuberculous pyothorax, tracheopleural fistula.
Contraindicated in patients with hepatic and renal injury, abnormal blood coagulation function and bleeding conditions. Before use, add appropriate amount of sodium chloride injection to dissolve. Intramuscular injection: local injection or spray inhalation, the dosage depends on the condition.
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 heteroenzyme activity, high stability, no self-cutting, high activity; in use, no non-specific enzyme slicing segments and self-slicing segments appear.
It is used for specific proteolytic digestion, protein sequencing, making peptide profiles, proteomics research, tryptic digestion of peptide segments on Z-D gel, and so on.
Physiological effect of Trypsin.
Trypsin belongs to the class of serine proteases that act specifically on the carboxyl terminus of Lys or Arg residues of peptide chains. Physiologically, they are involved in important processes such as metabolism, digestion, coagulation and other functions in animals.
In the field of cell biology, trypsin degrades proteins at the binding of cell membranes to petri dishes, causing the two to separate. And due to the tension of the cytoskeleton within the cell itself and the surface tension of the culture medium becomes spherical, thus realizing the digestion of the cell.
Product Method of Bulk Trypsin Powder.
Using bovine pancreas as raw material, trypsinogen is firstly produced, activated and then graded and precipitated by ammonium sulfate, then recrystallized and dialyzed product.
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