Chymotrypsin Chemical Properties

Melting point:

127°C

Density 

1.37[at 20℃]

vapor pressure 

0Pa at 25℃

storage temp. 

-20°C

solubility 

Reconstitute in 1mM HCl. Soluble at 10mg/ml in 1mM HCl. 2mM calcium chloride serves as a stabilizer. Store aliquoted solutions at -20°C for up to a week.

form 

salt-free, lyophilized powder

color 

white

Water Solubility 

125g/L at 25℃

Merck 

13,2282

LogP

-1.3 at 20℃

EPA Substance Registry System

Chymotrypsin (9004-07-3)

Safety Information

Hazard Codes 

Xn,B

Risk 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

HS Code 

35079090

Hazardous Substances Data

9004-07-3(Hazardous Substances Data)

MSDS

• Language:English Provider:Chymotrypsin
• Language:English Provider:SigmaAldrich

Chymotrypsin Usage And Synthesis

Chemical Properties

Lyophilized powder, dialyzed

Uses

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.

Uses

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

Uses

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].

Chymotrypsin(9004-07-3)Related Product Information

• Diethylstilbestrol
• Trypsin
• Proteinase K
• ENTEROKINASE
• Aprotinin
• CHYMOTRYPSINOGEN A
• 1,1,3,3-TETRAMETHYLBUTYL ISOCYANIDE
• Aluminum acetylacetonate
• Tosylmethyl isocyanide
• Cupric acetylacetonate
• Tris(2,4-pentanedionato)chroMiuM(III)
• N-BUTYLISOCYANIDE
• Benzyl isocyanide
• TRIS(2,2,6,6-TETRAMETHYL-3,5-HEPTANEDIONATO)EUROPIUM(III)
• TERT-BUTYL ISOCYANIDE
• Ferric acetylacetonate
• Ethyl isocyanoacetate
• SALCOMINE