Source: Swine (Bovine) pancreas
General description
Trypsin is a kind of serine proteolytic enzyme, with molecular weight of 23300 dalton, and is a single peptide chain composed of 223 amino acid residues. With rigorous specificity, the trypsin specifically acts on the peptide linkage constituted by the basic amino acid arginine and leucine. Enzyme easily autolyzes by itself, and its activation also reduces or loses gradually. It is easily soluble in the water, but insoluble in trichloromethane, ethanol, ether and glycerin, and the optimum PH is 8.0~9.0. When the PH is 1.8, it is hardly deactivated when boiled for a short time; if the salt is added into the hot solution, the protein will precipitate, and the enzyme action of filtrate cannot be seen, and Ca2+ plays the role in protecting and activating the trypsin.
The high purity Trypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration.
Application
  Clinical surgery used for all kinds of inflammation, ulcer, gangrene, wound, partial abscess caused by the atrophy hole, edema, hematoma and poisonous snake bite and other disease. In the surgery, it used for treat ringworm scabies and other skin disease. In the internal medicine, it used for empyema, emphysema, bronchitis, bronchial breathing and other disease. General intramuscular injection, also can inject to chest or to the hole of abscess atrophy tube, remove the pus washing or atomizing inhalation used for respiratory disorders. Besides, the treatment of diabetic complications, like the nephritis, treatment of bone disease and so on.
  As a food processing cutting big molecular protein.
  The hydrolysis of protein properties as reagent widely used in biology, medicine, food industry research and development, testing field.

Specification