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You are here:Home » Molecular Biology » MB-Enzymes, Protease (Proteinase, Peptidase) » Chymotrypsin, Human Pancreas

Chymotrypsin, Human Pancreas


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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. Chymotrypsinogen A is extracted from pancreatic tissue as a zymogen. Pancreatic extract contains approximately equal amounts of two forms of the zymogen, chymotrypsin A and chymotrypsin B. Chymotrypsin A may be activated to alpha, pi, beta, or gamma chymotrypsin. The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees, an inhibitor from potato, and organophosphorous compounds.
Catalog #C5070-08
ApplicationsSuitable for antigenic applications in immunological protocols. Shows no trypsin activity when assayed against N-benzyl-L-arginine-p-nitroanilide. Other applications have not been tested.
Rcommended DilutionsOptimal dilutions to be determined by the researcher.
Extinction coefficient 20.4
Specificity 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. A recent study has been made by Berezin and Martinek (1970) and Baumann et al. (1970).
Inhibitors The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees ( Birk 1961), an inhibitor from potato ( Ryan and Balls 1962), and organophosphorus compounds. Gel filtration of chymotrypsin removes autolysis products and other contaminants ( Yapel et al. 1966). The specificity of a-chloroketone as [[alpha]]-chymotrypsin inhibitor has been studied by Kumar and Hein (1970). Erlanger et al. (1970) report phenothiazine-N-carbonyl chloride to be specific for chymotrypsin inhibition.
Storage and StabilityLyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
CAS Number9004-07-3
SourceHuman pancreatic tissue
Purity~95% (SDS-PAGE)
FormSupplied as a salt free, lyophilized powder
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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