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S2628

Sigma-Aldrich

N-Succinyl-L-phenylalanine-p-nitroanilide

protease substrate, ≥98% (TLC), powder

Synonym(s):

Suc-Phe-pNA

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About This Item

Empirical Formula (Hill Notation):
C19H19N3O6
CAS Number:
2440-62-2
Molecular Weight:
385.37
EC Number:
219-472-6
MDL number:
MFCD00047721
UNSPSC Code:
12352204
PubChem Substance ID:
24899530
NACRES:
NA.32

product name

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

Quality Level

200

Assay

≥98% (TLC)

form

powder

solubility

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

storage temp.

−20°C

SMILES string

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

InChI key

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.

Biochem/physiol Actions

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.

Substrates

Reported to be a substrate for chymotrypsin.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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Articles

Chymotrypsin

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

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