Product Name: chymotrypsin
Chymotrypsin is a proteolytic enzyme that can preferentially hydrolyze the peptide bonds of tyrosine, phenylalanine and tryptophan containing L-type isomers. The optimal pH value of enzyme action is 8.0. Chymotrypsin activity can be inhibited by heavy metals and natural trypsin inhibitors to varying degrees.
Source: bovine pancreas or porcine pancreas
Properties: freeze dried powder
Activity: ≥ 1000u / Mg; ≥1500U/mg
character: white or quasi white lyophilized powder;
trypsin ≤ 1%,
drying loss ≤ 5.0%,
burning residue ≤ 2.5%;
storage: 2 ℃ – 8 ℃;
chymotrypsin ct11 ≥ 1000 USP U / mg
pakcing： 1g, 10g, 100g, bulk
The high-purity chymotrypsin produced by Shanghai Kekai Biotechnology Co., Ltd. is isolated and extracted from the pancreas and further prepared by affinity chromatography to remove the pollution of other remaining protease. The use of chymotrypsin includes: biochemical research. Protein decomposition and digestion. Proteolytic enzyme is used for protein hydrolysis without the presence of exogenous trypsin activity. It can decompose peptide bonds. The carboxyl end of the hydrolyzed peptide bond has aromatic or long hydrophobic chain (Tyr, Trp, Phe, Met) peptide bonds.
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