C4879

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

• Sinónimos: chymotrypsin A zymogen
• Número de CAS: 9035-75-0
• Número CE: 232-905-3
• Número MDL: MFCD00130483
• Código UNSPSC: 12352204
• NACRES: NA.54

Propiedades

• origen biológico: bovine pancreas
• Nivel de calidad: 200
• tpo: Type II
• Formulario: essentially salt-free, lyophilized powder
• actividad específica: ≥40 units/mg solid
• mol peso: 25,656 Da by calculation
• purificado por: 6× crystallization
• solubilidad: 1 mM HCl: soluble 10 mg/mL, clear, colorless
• Nº de acceso UniProt: P00767
• actividad extraña: α-chymotrypsin ≤1 U/mg (prior to activation by trypsin)
• temp. de almacenamiento: −20°C
• Información sobre el gen: cow ... CTRB1(618826)

Descripción

Descripción general

Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges.[1] It has an isoelectric pH of 8.97.

Aplicación

α-Chymotrypsinogen A from bovine pancreas has been used as model protein crystallization reproducibility studies.[2] It has also been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies.[3]

The enzyme from Sigma has been used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy.[4] It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems.[5] 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.[6]

Acciones bioquímicas o fisiológicas

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).[7] 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.[8]

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.

Definición de unidad

After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Otras notas

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

Información de seguridad

• Código de clase de almacenamiento: 11 - Combustible Solids
• Clase de riesgo para el agua (WGK): WGK 3
• Punto de inflamabilidad (°F): Not applicable
• Punto de inflamabilidad (°C): Not applicable
• Equipo de protección personal: Eyeshields, Gloves, type N95 (US)