ChemicalBook--->CAS DataBase List--->9035-75-0

9035-75-0

9035-75-0 Structure

9035-75-0 Structure
IdentificationBack Directory
[Name]

CHYMOTRYPSINOGEN A
[CAS]

9035-75-0
[Synonyms]

EC 3.4.21.1
CHYMOTRYPSINOGEN
CHYMOTRYPSINOGEN A
α-ChyMotrypinogenA
Chymotrypsinogen B
α-Chymotrypsinogen A
Molecularweightmarker/CH
ALPHA-CHYMOTRYPSINOGEN A
Chymotrypsinogen (crystal
ALPHA-CHYMOTRYPSIN TYPE II
CHYMOTRYPSINOGEN A, BOVINE
ALPHA-CHYMOTRYPSINOGEN A TYPE II
Native Bovine Chymotrypsinogen A
ChymotrypsinogenAExBovinePancreas
Native Bovine α-Chymotrypsinogen A
CHYMOTRYPSINOGEN (CRYSTAL, SALT FREE)
alpha-Chymotrypsinogen A from bovine pancreas
A-chymotrypsinogen A type ii from*bovine pancreas
Chymotrypsinogen A from bovine pancreas ca. 60 U/mg
ChyMotrypsinogen A froM bovine pancreas ca. 60 U/Mg lyophil. salt-free
[EINECS(EC#)]

232-905-3
[Molecular Formula]

NULL
[MDL Number]

MFCD00130483
Chemical PropertiesBack Directory
[storage temp. ]

−20°C
[solubility ]

Soluble in 0.001M HCl.
[form ]

essentially salt-free, lyophilized powder
[biological source]

bovine pancreas
[Specific Activity]

≥40units/mg solid
Safety DataBack Directory
[Safety Statements ]

22-24/25
[WGK Germany ]

3
[Storage Class]

11 - Combustible Solids
Hazard InformationBack Directory
[Uses]

Chymotrypsinogen A is used as a serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond, used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy. It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. The enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. In this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution.
[General Description]

Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges. It has an isoelectric pH of 8.97.
[Biochem/physiol Actions]

Chymotrypsinogen A requires limited proteolysis for its activation. Chymotrypsinogen A may be activated by trypsin and chymotrypsin (autolytic activation) to form m α, β, γ, δ and π chymotrypsin (depending upon the conditions of activation). Chymotrypsin is a protease that will preferentially cleave peptides on the carboxyl side of aromatic amino acids including tryptophan, tyrosine, and phenylalanine. It will also hydrolyze peptides on the carboxyl side of leucine, methionine, and alanine.
[in vivo]

Chymotrypsinogen has been used in tissue repair due to their ability to resolve inflammatory symptoms[2].

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