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Cat. No.
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CPE04
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Description
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The zymogen form of chymotrypsin. Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. Chymotrypsin catalyzes the hydrolysis of bonds of leucyl, methionyl, asparaginyl and glutamyl residues.
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Specific Activity
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≥ 1,000 USP units/mg material
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Unit definition
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That amount of activated zymogen that causes a decrease in absorbance at 237 nm of 0.0075 per minute at 25°C resulting from the hydrolysis of ATEE. (USP / NF unit)
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Specificity
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In addition to bonds involving aromatic amino acids, chymotrypsin catalyzes at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues.
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Optimum pH
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8.0
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Inhibitors
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The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees.
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Stability/Storage
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The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder when stored refrigerated.
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Product Specification
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Appearance
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White lyophilized powder
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Trypsin( USP)
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≤ 1%
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Loss on drying(60°C for 4 hours, USP)
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≤ 5.0%
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Solubility( USP)
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Soluble
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Residue on ignition( USP)
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≤ 2.5%
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Microbial Limits( USP)
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Pass
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pH(E.P.)
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3.0 – 5.0
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Product complies with USP28 and EP5.0.
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Download Datasheet:
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Abbr.: 
