Degradation
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α-Chymotrypsin

Degradation
Product Name
α-Chymotrypsin
CAS No.
9004-07-3
Chemical Name
α-Chymotrypsin
Synonyms
α-Chymotrypsin;A-CHYMOTRYPSIN;EC 3.4.21.1;ALPHA-CHYMOTRYPSIN;zolyse;zolyes;D03484;chymar;ec3445;ec3446
CBNumber
CB4167554
Molecular Formula
N/A
Formula Weight
0
MOL File
Mol file
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α-Chymotrypsin Property

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)
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Safety

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
3-10
TSCA 
Yes
HS Code 
35079090
Hazardous Substances Data
9004-07-3(Hazardous Substances Data)
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Hazard and Precautionary Statements (GHS)

Symbol(GHS)
Signal word
Danger
Hazard statements

H315Causes skin irritation

H317May cause an allergic skin reaction

H319Causes serious eye irritation

H334May cause allergy or asthma symptoms or breathing difficulties if inhaled

H335May cause respiratory irritation

Precautionary statements

P280Wear protective gloves/protective clothing/eye protection/face protection.

P302+P352IF ON SKIN: wash with plenty of soap and water.

P305+P351+P338IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continuerinsing.

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N-Bromosuccinimide Price

Sigma-Aldrich
Product number
SRP6509
Product name
Chymotrypsin from human pancreas
Purity
≥95% (SDS-PAGE)
Packaging
100μg
Price
$428
Updated
2024/03/01
Sigma-Aldrich
Product number
CHY5S
Product name
α-Chymotrypsin from bovine pancreas
Purity
≥40?units/mgprotein,vialof5?mg
Packaging
10vials
Price
$310
Updated
2024/03/01
Sigma-Aldrich
Product number
C9134
Product name
α-Chymotrypsin−Agarose from bovine pancreas
Purity
lyophilized powder, 2,000-3,500?units/g agarose (One ml gel will yield 65-120?units)
Packaging
50units
Price
$327
Updated
2024/03/01
Sigma-Aldrich
Product number
C9134
Product name
α-Chymotrypsin−Agarose from bovine pancreas
Purity
lyophilized powder, 2,000-3,500?units/g agarose (One ml gel will yield 65-120?units)
Packaging
100units
Price
$582
Updated
2024/03/01
Sigma-Aldrich
Product number
C8946
Product name
α-Chymotrypsin from human pancreas
Purity
lyophilized powder
Packaging
1VIAL
Price
$688
Updated
2024/03/01
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α-Chymotrypsin Chemical Properties,Usage,Production

Degradation

The rate and extent of insulin degradation by trypsin and α-Chymotrypsin were examined in vitro, and the initial sites of cleavage by α-Chymotrypsin were identified. The apparent Km for both enzymes was approximately the same, but the apparent Vmax for α-Chymotrypsin was 8.6 times greater. At a molar ratio of 172:1 (insulin: enzyme), chymotrypsin caused near-total loss of insulin within 40 min, while very little insulin was degraded by trypsin. Chymotrypsin appeared to cleave initially at the carboxyl side of the B26-Tyr and A19-Tyr residues, and additional cleavage at the B16-Tyr, B25-Phe, and A14-Tyr residue sites also occurred rapidly. Only two to three other susceptible bonds, which are not exposed at the surface of the insulin molecule, remained intact after the quenching of initial cleavage[1].

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+.

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.

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.

α-Chymotrypsin Preparation Products And Raw materials

Raw materials

Preparation Products

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α-Chymotrypsin Suppliers

TOKYO CHEMICAL INDUSTRY CO., LTD.
Tel
03-36680489
Fax
03-3668-0520
Email
Sales-JP@TCIchemicals.com
Country
Japan
ProdList
28387
Advantage
80
Nacalai Tesque, Inc.
Tel
--
Fax
--
Email
info-tech@nacalai.co.jp
Country
Japan
ProdList
6046
Advantage
75
Wako Pure Chemical Industries, Ltd.
Tel
--
Fax
--
Email
labchem-tec@wako-chem.co.jp
Country
Japan
ProdList
6819
Advantage
80
Kanto Chemical Co., Inc.
Tel
--
Fax
--
Email
reag-info@gms.kanto.co.jp
Country
Japan
ProdList
6756
Advantage
74
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View Lastest Price from α-Chymotrypsin manufacturers

BINBO BIOLOGICAL CO.,LTD
Product
Chymotrypsin 9004-07-3
Price
US $0.00/kg
Min. Order
1kg
Purity
99.8%
Supply Ability
1000 kg
Release date
2024-03-28
R&D Scientific Inc.
Product
Chymotrypsin 9004-07-3
Price
US $4500.00/Kg
Min. Order
1Kg
Purity
97
Supply Ability
500 Kg
Release date
2024-06-27
Shaanxi TNJONE Pharmaceutical Co., Ltd
Product
Alpha Chymotrypsin 9004-07-3
Price
US $0.00/kg
Min. Order
1kg
Purity
99%
Supply Ability
10000kg
Release date
2024-05-13

9004-07-3, α-ChymotrypsinRelated Search:


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