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Informacje o tej pozycji
Specific activity:
≥40 units/mg solid
Biological source:
bovine pancreas
Pomoc techniczna
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Pozwól nam pomócbiological source
bovine pancreas
Quality Segment
type
Type II
form
essentially salt-free, lyophilized powder
specific activity
≥40 units/mg solid
mol wt
25,656 Da by calculation
purified by
6× crystallization
solubility
1 mM HCl: soluble 10 mg/mL, clear, colorless
UniProt accession no.
foreign activity
α-chymotrypsin ≤1 U/mg (prior to activation by trypsin)
storage temp.
−20°C
Gene Information
cow ... CTRB1(618826)
General description
Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges. It has an isoelectric pH of 8.97.
Application
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.
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.
Biochem/physiol Actions
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.
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.
Other Notes
After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
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Klasa składowania
11 - Combustible Solids
Co się dzieje?
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
PPE (środki ochrony indywidualnej)
Eyeshields, Gloves, type N95 (US)
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