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Safety Information

C7762

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

Type I-S, essentially salt-free, lyophilized powder

Synonym(s):

α-chymotrypsin A and B, alpha-chymotrypsin

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About This Item

CAS Number:
9004-07-3
Enzyme Commission number:
3.4.21.1 (BRENDA, IUBMB)
EC Number:
232-671-2
MDL number:
MFCD00130481
UNSPSC Code:
12352204
eCl@ss:
42010112
NACRES:
NA.54

type

Type I-S

Quality Level

200

form

essentially salt-free, lyophilized powder

specific activity

≥40 units/mg protein

mol wt

25 kDa

purified by

3× crystallization

solubility

1 mM HCl: soluble 2.0 mg/mL, clear

UniProt accession no.

P00767

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

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Application

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.
The product has been used to investigate the inhibitory effect of several ether oligomers against the enzyme. It has also been used to cleave pro-phenoloxidase in order to estimate total phenoloxidase in haemolymph. Furthermore, the enzyme has been used as a positive control in chymotrypsin assays using salivary gland and anterior midgut extracts of Deraeocoris nigritulus.

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, as well as 10 mM of Cu2+ and Hg2+.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.

Unit Definition

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Preparation Note

Prepared free of autolysis products and low molecular weight contaminants.
The powder may be reconstituted in 1 mM HCl at 2 mg/mL concentration to form a clear solution.

Analysis Note

Minimum 85% protein
Protein determined by E1%/280

Other Notes

View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer

inhibitor

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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

Signal Word

Danger

Hazard Classifications

Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品

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Certificates of Analysis (COA)

Lot/Batch Number
0000407318
0000407319
0000407319
0000407318
0000407321

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. How should I prepare a solution of α-Chymotrypsin, Product C7762?

    It is recommended to reconstitute product C7762 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as both a stabilizer (and possibly an activator) of the enzyme.

  6. How can solutions of  α-Chymotrypsin, Product C7762, be stored?

    Stock solutions prepared in 1 mM HCl, containing 2 mM calcium chloride can be stored at -20 °C for about one week.

  7. What is the pH optimum for the enzyme, α-Chymotrypsin, Product C7762?

    The pH optimum is between pH 7.5-8.5.

  8. What is the molecular weight of alpha-chymotrypsin from bovine pancreas (Product No. C7762)?

    The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.  This information and the basic structure description of the enzyme can be found on our product information sheet (under Documents, above).

  9. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

Nathan W Bailey et al.
Biology letters, 7(2), 217-220 (2010-09-03)
Increased investment in immunity is expected to be beneficial under crowded conditions because of the greater risk of pathogen and parasite transmission, but the evolution of this facultative response relies on the ability to accurately assess social cues in the
Olivier Renaudet et al.
Organic letters, 6(3), 397-400 (2004-01-30)
[structure: see text] Hydroxyaromatic aldehydes and ketones were used as building blocks to prepare ether oligomers. An iterative two-step protocol involving Mitsunobu coupling and carbonyl reduction provided a protecting-group-free route with high yields. Activity screening of an 84-member library against
J A Hodgson et al.
Journal of general microbiology, 131(12), 3219-3227 (1985-12-01)
The effects of elevated temperature and of digestion with a variety of proteinases on the flocforming ability of flocculent strains of Saccharomyces cerevisiae, both genetically defined (FLO1 and FLO5) laboratory and genetically undefined brewing strains, have been determined. This has
Lakshmi Swarnalatha Jasti et al.
Biotechnology progress, 30(2), 317-323 (2014-01-23)
Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel
Digestive enzymes and stylet morphology of Deraeocoris nigritulus (Uhler)(Hemiptera: Miridae) reflect adaptations for predatory habits.
Boyd Jr, D. W.
Annals of the Entomological Society of America, 96(5), 667-671 (2003)
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Articles

Chymotrypsin

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

Protocols

Procedure for Enzymatic Assay of α-Chymotrypsin (EC 3.4.21.1)

Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.

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