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C4129

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

Type II, lyophilized powder, ≥40 units/mg protein

Synonym(s):

α-chymotrypsin A and B, alpha-chymotrypsin

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250 MG
HUF 19,800.00
500 MG
HUF 31,000.00
1 G
HUF 55,600.00
10 G
HUF 345,000.00

HUF 19,800.00


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250 MG
HUF 19,800.00
500 MG
HUF 31,000.00
1 G
HUF 55,600.00
10 G
HUF 345,000.00

About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
42010112
NACRES:
NA.54

HUF 19,800.00


Please contact Customer Service for Availability

type

Type II

Quality Level

form

lyophilized powder

specific activity

≥40 units/mg protein

mol wt

25 kDa

composition

protein, ≥85%

color

white to off-white

UniProt accession no.

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

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Application

The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE).[1]

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+.
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

Produced from 3× crystallized chymotrypsinogen

Analysis Note

Protein determined by E1%/280

Other Notes

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

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Antonio Jesús Vizcaíno et al.
Marine drugs, 18(6) (2020-06-24)
This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species
K Y Jiang et al.
Biochimica et biophysica acta, 1433(1-2), 198-209 (1999-08-14)
Chemical glycosylation of bovine alpha-chymotrypsin, by a glucosamine adduct on the carboxyl group, results in the modification of its catalytic activity. The structural alterations of alpha-chymotrypsin resulting from its glycosylation are studied by immobilized metal-ion affinity chromatography (IMAC) and immobilized
Ines Atuh Ngoh et al.
Experimental parasitology, 218, 107969-107969 (2020-08-29)
Invasion of human red blood cells (RBCs) by Plasmodium parasites is a crucial yet poorly characterised phenotype. Two-color flow cytometry (2cFCM) promises to be a very sensitive and high throughput method for phenotyping parasite invasion. However, current protocols require high
Xingchen Chen et al.
Marine drugs, 17(12) (2019-12-18)
Serine proteases play pivotal roles in normal physiology and a spectrum of patho-physiological processes. Accordingly, there is considerable interest in the discovery and design of potent serine protease inhibitors for therapeutic applications. This led to concerted efforts to discover versatile
Olivia Ogilvie et al.
MethodsX, 7, 101076-101076 (2020-10-10)
Mass spectrometry (MS) is an emerging method to determine the accurate concentration of immunogenic gluten peptides. It is of interest to quantify specific peptides within the gluten peptidome due to the role they play in the activation of the celiac

Articles

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

Protocols

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.

Chromatograms

application for HPLC

Questions

1–5 of 5 Questions  
  1. What is the Department of Transportation shipping information for this product?

    1 answer
    1. 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.

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  2. How can solutions of alpha chymotrypsin (Product No. C4129) be stored?

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

      Helpful?

  3. What is the pH optimum for the enzyme, Product No. C4129?

    1 answer
    1. 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).

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  4. How do you recommend preparing a solution of Product No. C4129?

    1 answer
    1. It is recommended to reconstitute Product No. C4129 in 1 mM hydrochloric acid containing 2 mM calcium chloride. The calcium functions as a stabilizer, and possibly an activator, of the enzyme.

      Helpful?

  5. What is the molecular weight of alpha-chymotrypsin from bovine pancreas, product C4129?

    1 answer
    1. The molecular weight of alpha chymotrypsin, reported in the literature, is approximately 25 kDa.

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