DESCRIPTION
Chymotrypsin is a proteolytic enzyme, which preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan. The optimum pH is 8.0.The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees.
Linzyme ultrapure Chymotrypsin is extracted from bovine pancreas and has been further purified by an affinity chromatography to remove trace contaminating proteases.
Function of Chymotrypsin
Chymotrypsin is widely used to treat kinds of inflammation,inflammatory edema,hematoma,postoperative adhesion,ulcer,thrombus and so on.It has effect on chronic bronchitis,bronchial asthma, gastritis,cervicitis,pelvic inflammatory disease,otitis,keratitis,prostatitis,venous embolism and brain thrombosis
Chymotrypsin is also called chymotrypsinogen.
Chymotrypsin is the endopeptidase extracted and separated from the fresh pancreas of cows (or pigs).
Primary structure and spatial structure of α- Chymotrypsin have been clearly explained, which is a single peptide chain composed of 245 amino acid residues, with 5 pairs of disulfide linkage in the molecule.
Chymotrypsin is white and light yellow crystal or amorphous powder, and easily soluble in the water, but insoluble in organic solvent. Relative molecular mass is 24000, and the optimum PH is 8~9.
Chymotrypsin is stable at a dry state, but will be quickly deactivated in water solution, most stable in the water solution with PH3~4. When it acts on the protein, Chymotrypsin will hydrolyze the peptide bond formed by the carboxyl of L-tyrosine and L-phenylalanine in priority.