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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

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Synonym(s):
TLCK-Chymotrypsin
CAS Number:
9004-07-3
Enzyme Commission number:
3.4.21.1 (BRENDA, IUBMB)
EC Number:
232-671-2
MDL number:
MFCD00130481
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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α-Chymotrypsin from bovine pancreas (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein

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C3142

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas Type I-S, essentially salt-free, lyophilized powder

Sigma-Aldrich

C7762

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas Type II, lyophilized powder, ≥40 units/mg protein

Sigma-Aldrich

C4129

α-Chymotrypsin from bovine pancreas

α-Chymotrypsin from bovine pancreas suitable for protein sequencing, salt-free, lyophilized powder

Sigma-Aldrich

C6423

α-Chymotrypsin from bovine pancreas

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

lyophilized powder

form

salt-free, lyophilized powder

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥40 units/mg protein

specific activity

-

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

solubility

1 mM HCl: soluble 10 mg/mL, clear

solubility

1 mM HCl: soluble 2.0 mg/mL, clear

solubility

-

solubility

-

UniProt accession no.

P00767

UniProt accession no.

P00767

UniProt accession no.

P00767

UniProt accession no.

P00767

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

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

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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