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C4129

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

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

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Synonym(s):
α-chymotrypsin A and B, alpha-chymotrypsin
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42010112

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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This Item
C7762C3142CHY5S
specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

Quality Level

300

Quality Level

200

Quality Level

200

Quality Level

200

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

color

white to off-white

color

-

color

-

color

-

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

solid

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).

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

signalword

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

11 - Combustible Solids

wgk_germany

WGK 1

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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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
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Shannon Gwala et al.
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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
Olivia Ogilvie et al.
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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

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