Ugrás a tartalomra
Merck

C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Szinonimák:

chymotrypsin A zymogen

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54

biológiai forrás

bovine pancreas

Minőségi szint

típus

Type II

form

essentially salt-free, lyophilized powder

specifikus aktivitás

≥40 units/mg solid

molekulatömeg

25,656 Da by calculation

tisztítva

6× crystallization

oldhatóság

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

UniProt elérési szám

idegen aktivitás

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

tárolási hőmérséklet

−20°C

Géninformáció

Általános leírás

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

Alkalmazás

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.

Biokémiai/fiziológiai hatások

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.

Egység definíció

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

Egyéb megjegyzések

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, type N95 (US)


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

On the activation of bovine chymotrypsinogen A. Conformational isomerization of alpha1-and kappa-chymotrypsin and their autolytic conversion to alpha-and gamma-chymotrypsin.
Sharma SK and Hopkins TR
The Journal of Biological Chemistry, 253(9), 3055-3061 (1978)
Structural basis of IgE binding to alpha-and gamma-gliadins: Contribution of disulfide bonds and repetitive and nonrepetitive domains
Mameri H, et al.
Journal of Agricultural and Food Chemistry, 63(29), 6546-6554 (2015)
9.1 Proteases: Facilitating a Difficult Reaction
Biochemistry (5th Edition) (2002)
Peter M Tessier et al.
Biophysical journal, 82(3), 1620-1631 (2002-02-28)
Weak protein interactions are often characterized in terms of the osmotic second virial coefficient (B(22)), which has been shown to correlate with protein phase behavior, such as crystallization. Traditional methods for measuring B(22), such as static light scattering, are too
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

Cikkek

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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