Advantages at a glance
- Activity: min. 400 U/mg
- Appearance: off-white powder
- Loss on drying: max. 5%
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Product information "alpha-Chymotrypsin (EC 3.4.21.1) from Porcine"
alpha-Chymotrypsin is a serine peptidase that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Leu) on the carboxyl end of the bond. Ca2+ activates and stabilizes the enzyme. The enzyme has 241 amino acid residues in total contained in three polypeptide chains (A chain: 13 amino acids; B chain: 131 amino acids, and C chain: 97 amino acids) linked by disulfide bridges.
alpha-Chymotrypsin is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF) >, N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK) >, chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10mM Cu2+ and Hg2+.
Specifications:
Activity: min. 400 U/mg
Appearance: off-white powder
pH: 4.0 - 5.0
Loss on drying: max. 5%
MW = about 25,000 g/mol
Source: from porcine
Application:
digestion of proteins/peptidesUnits:
One unit is defined as the amount of enzyme that causes a decrease in absorbance at 237nm of 0.0075 per minute at 25°C resulting from the hydrolysis of ATEE (NF/USP unit).Source:
porcineSafety Information:
Classification:
Documents:
CertificateCategory List