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Safety Information

C9134

Sigma-Aldrich

α-Chymotrypsin−Agarose from bovine pancreas

lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)

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About This Item

Enzyme Commission number:
3.4.21.1 (BRENDA, IUBMB)
MDL number:
MFCD00130481
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

200

form

lyophilized powder

specific activity

2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)

mol wt

25 kDa

UniProt accession no.

P00767

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

Related Categories

Application

α-Chymotrypsin agarose from bovine pancreas has been used to study the purification and characterization of glucoamylase. α-Chymotrypsin agarose from bovine pancreas has also been used in a study to investigate molecular modeling for the design of a biomimetic chimeric ligand.

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

Unit Definition

One unit will hydrolyze 1.0 μmole of N-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 8.0 at 30 °C.

Physical form

Stabilized with lactose

Analysis Note

Protein determined by A1%/280

inhibitor

Product No.
Description
Pricing

A2504

6-Aminocaproic acid, ≥99% (titration), powder

A7824

6-Aminocaproic acid, BioUltra, ≥99%

D0879

Diisopropylfluorophosphate

L2023

Leupeptin trifluoroacetate salt, ≥90% (HPLC), microbial

T9777

Trypsin-chymotrypsin inhibitor from Glycine max (soybean), lyophilized powder

A1153

Aprotinin from bovine lung, lyophilized powder, 3-8 TIU/mg solid

P7626

Phenylmethanesulfonyl fluoride, ≥98.5% (GC)

B1552

Bromoenol lactone, ≥98% (TLC)

A9024

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A6150

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A9285

α1-Antichymotrypsin from human plasma, ≥92.5% (SDS-PAGE), lyophilized powder

T4376

N-p-Tosyl-L-phenylalanine chloromethyl ketone, ≥97% (TLC), powder

C7268

Chymostatin, microbial

substrate

Product No.
Description
Pricing

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H317,H319,H334,H335

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

C9134-100UN:
C9134-5UN:
C9134-25UN:
C9134-VAR:
C9134-50UN:
C9134-BULK:
C9134-10UN:

Certificates of Analysis (COA)

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Saleh A Mohamed et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 140(1), 73-80 (2004-12-29)
The present study analyzed the existence of carbohydrases in camel pancreas compared to some other ruminants. Disaccharidases (maltase, cellobiase, lactase, trehalase and sucrase), glucoamylase and alpha-amylase were detected in pancreas of camel, sheep, cow and buffalo. Enzyme levels in sheep
Ke Xu et al.
The Journal of biological chemistry, 283(49), 34337-34344 (2008-10-11)
The clinical severity of Osteogenesis Imperfecta (OI), also known as the brittle bone disease, relates to the extent of conformational changes in the collagen triple helix induced by Gly substitution mutations. The lingering question is why Gly substitutions at different
N E Labrou et al.
Biotechnology and bioengineering, 63(3), 322-332 (1999-04-01)
Molecular modeling was employed for the design of a biomimetic chimeric ligand for L-lactate dehydrogenase (LDH). This ligand is an anthraquinone monochlorotriazinyl dye comprising two moieties: (a) the ketocarboxyl biomimetic moiety, 2-(4-aminophenyl)-ethyloxamic acid, linked on the monochlorotriazine ring, mimicking the
Y Gao et al.
The Journal of biological chemistry, 276(13), 9838-9845 (2001-01-20)
Dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine (O-GlcNAc) on Ser/Thr residues is ubiquitous in higher eukaryotes and is analogous to protein phosphorylation. The enzyme for the addition of this modification, O-GlcNAc transferase, has been cloned from several
Vincent Dechavanne et al.
Protein expression and purification, 87(2), 100-110 (2012-11-14)
The proteasome is a multicatalytic protease complex present in all eukaryotic cells, which plays a critical role in regulating essential cellular processes. During the immune response to pathogens, stimulation by γ interferon induces the production of a special form of
View All Related Papers

Articles

Chymotrypsin

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

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