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CHY5S Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

≥40 units/mg protein, vial of 5 mg

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Biochemicals and Reagents, Enzyme Class Index, Enzymes, Inhibitors, and Substrates More...
description   aseptically filled
type   Type IV-S
mol wt   25 kDa
composition   protein, ≥85% UV
packaging   vial of 5 mg
storage temp.   −20°C
Gene Information   cow ... CTRB1(618826)

Description

Application

α-Chymotrypsin from bovine has been used in a study to inform proteasome inhibition in order to advance anticancer research. α-Chymotrypsin from bovine has also been used in a study that functionalized surface anchored poly(methylhydrosiloxane) thin films on oxidized silicon wafers.

The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration.

α-Chymotrypsin from bovine pancreas has been used:
• as a supplement for the collection of semen into Tris diluent
• as one of the proteases in the analysis of major histocompatibility complex (MHC) class II protease sensitivity assay
• as a component in YEPD broth for biofilm dispersion assay
• in the preparation of chitinase–chymotrypsin–DMSO buffer (CCD buffer) for enzymatic digestion of larvae

Biochem/physiol Actions

α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.

A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.

Unit Definition

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Analysis Note

Protein determined by A1%/280

Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
GC3050000

Documents

Certificate of Analysis

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Certificate of Origin

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Protocols & Articles

Protocols

Procedure for Enzymatic Assay of α-Chymotrypsin (EC 3.4.21.1)

This procedure may be used for the determination of α‑Chymotrypsin activity using N-Benzoyl-L-tyrosine ethyl ester (BTEE) as the substrate. It is not to be used to assay α‑Chymotrypsin agarose (Catal...
Keywords: Extinction coefficient

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Metabolomics, Molecular biology

Peer-Reviewed Papers
15

References

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