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. It 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. It 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, it will hydrolyze the peptide bond formed by the carboxyl of L-tyrosine and L-phenylalanine in priority.
The high purity Chymotrypsin of Enzymeking Biotechnology Co., Ltd. is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration.
Enzymeking Biotechnology Co., Ltd.
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