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S2628

Sigma-Aldrich

N-Succinyl-L-phenylalanine-p-nitroanilide

protease substrate, ≥98% (TLC), powder

Synonyme(s) :

Suc-Phe-pNA

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About This Item

Formule empirique (notation de Hill):
C19H19N3O6
Numéro CAS:
Poids moléculaire :
385.37
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
ID de substance PubChem :
Nomenclature NACRES :
NA.32

product name

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

Niveau de qualité

Pureté

≥98% (TLC)

Forme

powder

Solubilité

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

Température de stockage

−20°C

Chaîne SMILES 

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

Clé InChI

KNBLWBFJHZHYFG-INIZCTEOSA-N

Application

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.

Actions biochimiques/physiologiques

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.

Substrats

Reported to be a substrate for chymotrypsin.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
Cyclopeptide alkaloids of Ziziphus oxyphylla Edgw as novel inhibitors of alpha-glucosidase enzyme and protein glycation
Choudhary MI, et al.
Phytochemistry Letters, 4(4), 404-406 (2011)
[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)
K Ashizawa et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 121(1), 77-83 (1999-02-11)
We investigated the effects of various protease substrates on the motility of demembranated fowl spermatozoa. In the presence of ATP, the motility of demembranated spermatozoa was vigorous at 30 degrees C, but decreased markedly following the addition of protease substrates

Articles

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

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