9004-07-3

Basic information

• Product Name: Chymotrypsin
• Synonyms: alfapsin;alphachymar;alpha-chymarophth;alpha-chymotrypsinfrombovinepancreas;avazyme;catarase;chymar;chymolase
• CAS NO: 9004-07-3
• Molecular Weight: 0
• EINECS: 232-671-2
• Product Categories: Application Index;ProteasesEnzyme Class Index;3.4.x.x Peptidases;Chymotrypsin, alpha-Application Index;ProteasesApplication Index;Protein SequencingEnzymes, Inhibitors, and Substrates;Proteolytic Enzymes and Substrates;Proteolytic EnzymesEnzyme Class Index;Selective Proteolytic Enzymes;3.x.x.x Hydrolases;Proteases&Protein Sequencing;ProteasesEnzymes, Inhibitors, and Substrates;Enzyme Class Index;Chymotrypsin, alpha-Mass Spectrometry;Enzymatic and Chemical Protein Cleavage;Proteases for Cleavage of ProteinsEnzymes, Inhibitors, and Substrates;API;enzyme;Lyophilized;White lyophilized
• Mol File: 9004-07-3.mol
• Article Data: 0

Chemical Properties

• Melting Point: 127°C
• Appearance: white/salt-free, lyophilized powder
• Density: 1.37[at 20℃]
• Vapor Pressure: 0Pa at 25℃
• Storage Temp.: 2-8°C
• Solubility: Reconstitute in 1mM HCl. Soluble at 10mg/ml in 1mM HCl. 2mM calc
• Water Solubility: 125g/L at 25℃
• Merck: 13,2282
• CAS DataBase Reference: Chymotrypsin(CAS DataBase Reference)
• NIST Chemistry Reference: Chymotrypsin(9004-07-3)
• EPA Substance Registry System: Chymotrypsin(9004-07-3)

Safety Data

• Hazard Codes: Xn,B
• Statements: 36/37/38-42/43-42
• Safety Statements: 26-36-36/37-24-22
• WGK Germany: 3
• RTECS: GC3050000
• F: 3-10
• TSCA: Yes
• Hazardous Substances Data: 9004-07-3(Hazardous Substances Data)

Usage

Chemical Properties

Lyophilized powder, dialyzed

Uses

Different sources of media describe the Uses of 9004-07-3 differently. You can refer to the following data:
1. 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.
2. The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration.
3. α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin.

General Description

Chymotrypsin (Chymar) is extractedfrom mammalian pancreas and is used in cataractsurgery. A dilute solution is used to irrigate the posteriorchamber of the eye to dissolve the fine filaments that holdthe lens.

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, α2-macroglobulin, 10 mM Cu2+ and Hg2+.

Purification Methods

α-Chymotrypsin is crystallised twice from four-tenths saturated ammonium sulfate solution, then dissolved in 1mM HCl and dialysed against 1mM HCl at 2-4o. The solution is stored at 2o [Lang et al. J Am Chem Soc 80 4923 1958].