α-Chymotrypsin
Synonym(s):CLCR;CTRC;CTRC_HUMAN;ELA 4;Elastase 4
- CAS NO.:9004-07-3
- Empirical Formula: N/A
- Molecular Weight: 0
- MDL number: MFCD00130481
- EINECS: 232-671-2
- SAFETY DATA SHEET (SDS)
- Update Date: 2024-11-01 13:17:44
What is α-Chymotrypsin?
Absorption
No pharmacokinetic data available.
Toxicity
No toxicokinetic data available.
Chemical properties
Lyophilized powder, dialyzed
The Uses of α-Chymotrypsin
The enzyme from Sigma has been used to assess the effect of limited proteolysis with α-chymotrypsin on the sperm penetration.
The Uses of α-Chymotrypsin
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 Uses of α-Chymotrypsin
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.
Indications
No therapeutic indications.
Background
Chymotrypsin (EC 3.4.21.1) is a digestive enzyme that promotes proteolysis, or the breakdown of proteins and polypeptides. It is a serine protease synthesized in the pancreas and is a vital component in the pancreatic juice. Like most proteolytic enzymes, chymotrypsin is activated from its inactive zymogen precursor, chymotrypsinogen, in presence of Trypsin. Chymotrypsin is the most abundant pancreatic proteases that represent up to 10-20% of the total protein synthesized by the exocrine pancreas . Chymotrypsin contains both the catalytic triad and oxyanion hole, and the tertiary structure of chymotrypsin is similar to 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+.
Mechanism of action
The general mechanism for chymotrypsin is the classic serine protease mechanism. Hydrolytic proteolysis by α-chymotrypsin begins with an initial nucleophilic attack on the peptide bond by Ser 195, activated by deprotonation by His 57. This leads to forming a tetrahedral intermediate, stabilized by the amide groups of Ser 195 and Gly 193. The subsequent collapse of this intermediate, assisted by protonation of the leaving group by His 57 and Asp 102, leads to an acyl-enzyme intermediate. Activation of a water molecule by His 57 and Asp 102 facilitates hydrolysis of this intermediate, resulting in the reformation of the catalytically active serine residue and the release of the product facilitated by protonation with His 57.
Pharmacokinetics
Chymotrypsin is a digestive enzyme synthesized in the pancreas that plays an essential role in proteolysis, or the breakdown of proteins and polypeptides. As a component in the pancreatic juice, chymotrypsin aids in the digestion of proteins in the duodenum by preferentially cleaving peptide amide bonds.
Metabolism
No pharmacokinetic data available.
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].
References
[1] R J Schilling, A K Mitra. “Degradation of insulin by trypsin and alpha-chymotrypsin.” Pharmaceutical Research 8 6 (1991): 721–7.
Properties of α-Chymotrypsin
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 |
EPA Substance Registry System | Chymotrypsin (9004-07-3) |
Safety information for α-Chymotrypsin
Signal word | Danger |
Pictogram(s) |
Exclamation Mark Irritant GHS07 Health Hazard GHS08 |
GHS Hazard Statements |
H315:Skin corrosion/irritation H317:Sensitisation, Skin H319:Serious eye damage/eye irritation H334:Sensitisation, respiratory H335:Specific target organ toxicity, single exposure;Respiratory tract irritation |
Precautionary Statement Codes |
P280:Wear protective gloves/protective clothing/eye protection/face protection. P302+P352:IF ON SKIN: wash with plenty of soap and water. P305+P351+P338:IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continuerinsing. |
Computed Descriptors for α-Chymotrypsin
Abamectin manufacturer
Meteoric Biopharmaceuticals Pvt. Ltd.
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