C9134
α-Chymotrypsin−Agarose from bovine pancreas
lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)
Product Name
α-Chymotrypsin−Agarose from bovine pancreas, lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)
biological source
bovine pancreas
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.
storage temp.
−20°C
Quality Level
Gene Information
cow ... CTRB1(618826)
Related Categories
Analysis Note
Protein determined by A1%/280
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.
Other Notes
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Regulatory Information
低风险生物材料
动植物源性产品
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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
Yukiko Taketani et al.
Bioscience, biotechnology, and biochemistry, 75(10), 1872-1879 (2011-10-08)
Thioredoxin (TRX) catalyzes the reduction of disulfide bonds in proteins via the NADPH-dependent thioredoxin reductase system. Reducing the disulfide bonds of allergenic proteins in food by TRX lowers the allergenicity. We established in this study a method to prepare TRX-enriched
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
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
Steven W Millward et al.
ACS chemical biology, 2(9), 625-634 (2007-09-27)
There is a pressing need for new molecular tools to target protein surfaces with high affinity and specificity. Here, we describe cyclic messenger RNA display with a trillion-member covalent peptide macrocycle library. Using this library, we have designed a number
Articles
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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