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C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Sinónimos:

chymotrypsin A zymogen

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About This Item

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

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)

Categorías relacionadas

Descripción general

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

Aplicación

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

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). 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.
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

Aplicación

Referencia del producto
Descripción
Precios

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)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Curtiss P Schneider et al.
The journal of physical chemistry. B, 115(22), 7447-7458 (2011-05-17)
L-Arginine hydrochloride is a very important aggregation suppressor for which there has been much attention given regarding elucidating its mechanism of action. Little consideration, however, has been given toward other salt forms besides chloride, even though the counterion likely imparts
Curtiss P Schneider et al.
The journal of physical chemistry. B, 113(7), 2050-2058 (2009-02-10)
The relatively new technique of vapor pressure osmometry was utilized to determine the preferential interaction of five common solution additives (arginine HCl, guanidine HCl, glycerol, glucose, and urea) using three different model proteins (BSA, lysozyme, and alpha-chymotrypsinogen). Results for guanidine
Effect of real-world sounds on protein crystallization
Zhang CY, et al.
International Journal of Biological Macromolecules, 112, 841-851 (2018)
Pedro P Madeira et al.
Journal of chromatography. A, 1190(1-2), 39-43 (2008-04-02)
Distribution coefficients of randomly selected proteins were measured in aqueous two-phase systems (ATPSs) formed by different combinations of Dextran-75 (Dex), Ficoll-70, polyethylene glycol-8000 (PEG), hydroxypropyl starch-100 (PES), and Ucon50HB5100 (Ucon, a random copolymer of ethylene glycol and propylene glycol) at
Shujun Bai et al.
Journal of pharmaceutical sciences, 94(9), 2030-2038 (2005-07-30)
Fourier transform infrared (FTIR) spectroscopy is a powerful tool for monitoring structural changes in lyophilized protein formulations. However, direct measurement of IR spectra requires significant handling time and effort. The possibility of using near infrared (NIR) spectroscopy as a rapid
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Artículos

HPLC Analysis of Proteins on TSKgel® BioAssist S

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins on Proteomix® SCX-NP5

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX-NP5: Affect of pH

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX: Affect of Particle Size

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

Ver todo

Chromatograms

application for HPLC

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