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Documenti fondamentali

S2628

Sigma-Aldrich

N-Succinyl-L-phenylalanine-p-nitroanilide

protease substrate, ≥98% (TLC), powder

Sinonimo/i:

Suc-Phe-pNA

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About This Item

Formula empirica (notazione di Hill):
C19H19N3O6
Numero CAS:
Peso molecolare:
385.37
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
ID PubChem:
NACRES:
NA.32

Nome del prodotto

N-Succinyl-L-phenylalanine-p-nitroanilide, protease substrate

Livello qualitativo

Saggio

≥98% (TLC)

Stato

powder

Solubilità

dioxane: 25 mg/mL, clear, colorless to faintly yellow

Temperatura di conservazione

−20°C

Stringa SMILE

OC(=O)CCC(=O)N[C@@H](Cc1ccccc1)C(=O)Nc2ccc(cc2)N(=O)=O

InChI

1S/C19H19N3O6/c23-17(10-11-18(24)25)21-16(12-13-4-2-1-3-5-13)19(26)20-14-6-8-15(9-7-14)22(27)28/h1-9,16H,10-12H2,(H,20,26)(H,21,23)(H,24,25)/t16-/m0/s1
KNBLWBFJHZHYFG-INIZCTEOSA-N

Applicazioni

N-Succinyl-L-phenylalanine-p-nitroanilide has been used as a substrate for the hydrolytic activity of chymotrypsin and molar absorptive experiments. It has also been used for monitoring in vitro α-chymotrypsin inhibition assay.

Azioni biochim/fisiol

N-Succinyl-L-phenylalanine-p-nitroanilide, a substrate for the hydrolytic activity of chymotrypsin, forms a yellow chromophore, p-nitroaniline, which can be measured spectrophotometrically at 410 nm.

Substrati

Reported to be a substrate for chymotrypsin.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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Certificati d'analisi (COA)

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Isabel Pastor et al.
The journal of physical chemistry. B, 115(5), 1115-1121 (2010-12-31)
Traditionally, studies on the diffusion-controlled reaction of biological macromolecules have been carried out in dilute solutions (in vitro). However, in an intracellular environment (in vivo), there is a high concentration of macromolecules, which results in nonspecific interactions (macromolecular crowding). This
E Iu Maksareva et al.
Bioorganicheskaia khimiia, 21(1), 24-27 (1995-01-01)
Subtilisin Carlsberg (E.C. 3.4.21.14) catalyzes the hydrolysis of N-succinyl-L-phenylalanine p-nitroanilide in solid-state solvent-free hydrated protein-substrate mixtures. This process needs a certain critical degree of hydration of the protein molecule which is attained at the relative water vapour pressure (p/ps) above
Mercury (II) binds to both of chymotrypsin's histidines, causing inhibition followed by irreversible denaturation/aggregation
Stratton A, et al.
Protein Science, 26(2), 292-305 (2017)
V V Mozhaev et al.
Biochemistry and molecular biology international, 34(1), 191-199 (1994-08-01)
Biocatalytic transformations in reversed micelles formed by anionic surfactant Aerosol OT in octane have been studied at high pressures by an example of alpha-chymotrypsin-catalyzed hydrolysis of N-carbobenzoxy-L-tyrosine p-nitrophenyl ester and N-succinyl-L-phenylalanine p-nitroanilide. For the first time it has been found
[ON THE DETERMINATION OF TRYPSIN AND CHYMOTRYPSIN WITH AMINO-P-NITROANILIDES].
W NAGEL et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 340, 1-10 (1965-01-01)

Articoli

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

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