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Safety Information

C3142

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

(TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein

Synonym(s):

TLCK-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

Quality Level

200

type

Type VII

form

essentially salt-free, lyophilized powder

specific activity

≥40 units/mg protein

mol wt

25 kDa

solubility

1 mM HCl: soluble 10 mg/mL, clear

UniProt accession no.

P00767

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

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Application

α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme.

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+.
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

TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.

Analysis Note

Protein determined by A1%/280

Other Notes

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

inhibitor

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Description
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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

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
0000313642
0000313641
0000313641
0000313642
SLCK9188

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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. What is the molecular weight of alpha-chymotrypsin from bovine pancreas (Product No. C3142)?

    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) at our website.

  6. How do you recommend preparing a solution of Product No. C3142?

    It is recommended to reconstitute Product No. C3142 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as both a stabilizer (and possibly an activator) of the enzyme.

  7. How can solutions of alpha-chymotrypsin (Product No. C3142) be stored?

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

  8. What is the pH optimum for the enzyme, Product No. C3142?

    The pH optimum for alpha-chymotrypsin is between pH 7.5-8.5. Please see the following reference: Wilcox, P.E., Chymotrypsingogens-chymotrypsins, Methods in Enzymology, 19, 64-80 (1970).

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

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The Journal of biological chemistry, 276(42), 38893-38898 (2001-08-10)
The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine alpha-chymotrypsin at 2.1- and 3.0-A resolution, respectively. PMP-C is a potent bovine alpha-chymotrypsin inhibitor whereas native PMP-D2 is
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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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