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Merck

C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Synonym(e):

chymotrypsin A zymogen

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About This Item

CAS-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

bovine pancreas

Typ

Type II

Form

essentially salt-free, lyophilized powder

Spezifische Aktivität

≥40 units/mg solid

Mol-Gew.

25,656 Da by calculation

Aufgereinigt durch

6× crystallization

Löslichkeit

1 mM HCl: soluble 10 mg/mL, clear, colorless

UniProt-Hinterlegungsnummer

Fremdaktivität

α-chymotrypsin ≤1 U/mg (prior to activation by trypsin)

Lagertemp.

−20°C

Angaben zum Gen

Verwandte Kategorien

Allgemeine Beschreibung

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

Anwendung

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.

Biochem./physiol. Wirkung

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.

Einheitendefinition

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

Sonstige Hinweise

Finden Sie mehr Informationen zu Chymotrypsin auf unserer 'Enzyme-Explorer'-Webseite.

Anwendung

Produkt-Nr.
Beschreibung
Preisangaben

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Simulation of the activation of alpha-chymotrypsin: Analysis of the pathway and role of the propeptide
Matrai J, et al.
Protein Science, 13(12), 3139-3150 (2004)
Angelina Angelova et al.
International journal of pharmaceutics, 454(2), 625-632 (2013-06-25)
Defining appropriate delivery strategies of therapeutic proteins, based on lipid nanoparticulate carriers, requires knowledge of the nanoscale organization that determines the loading and release properties of the nanostructured particles. Nanoencapsulation of three cationic proteins (human brain-derived neurotrophic factor (BDNF), α-chymotrypsinogen
Rob Haselberg et al.
Analytica chimica acta, 678(1), 128-134 (2010-09-28)
A capillary electrophoresis-mass spectrometry (CE-MS) method using sheath liquid electrospray ionization interfacing was studied and optimized for the analysis of intact basic proteins. To prevent protein adsorption, capillaries with a noncovalent positively charged coating were utilized. Capillaries were coated by
Nafees Rahman et al.
Biomaterials, 31(32), 8262-8270 (2010-08-06)
The developmental potential of pluripotent stem cells is influenced by their local cellular microenvironment. To better understand the role of vascular endothelial growth factor (VEGFA) in the embryonic cellular microenvironment, we synthesized an artificial stem cell niche wherein VEGFA was
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

Artikel

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

Chromatograms

application for HPLC

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