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G2505

Sigma-Aldrich

N-Glutaryl-L-phenylalanine p-nitroanilide

protease substrate

Synonym(s):

Glutaryl-L-phenylalanine 4-nitroanilide

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About This Item

Empirical Formula (Hill Notation):
C20H21N3O6
CAS Number:
Molecular Weight:
399.40
Beilstein:
2919832
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.83

Assay

≥98% (HPLC)

form

powder

solubility

methanol with 1 M NH4OH: 50 mg/mL, clear to slightly hazy

storage temp.

−20°C

SMILES string

OC(=O)CCCC(=O)N[C@@H](Cc1ccccc1)C(=O)Nc2ccc(cc2)[N+]([O-])=O

InChI

1S/C20H21N3O6/c24-18(7-4-8-19(25)26)22-17(13-14-5-2-1-3-6-14)20(27)21-15-9-11-16(12-10-15)23(28)29/h1-3,5-6,9-12,17H,4,7-8,13H2,(H,21,27)(H,22,24)(H,25,26)/t17-/m0/s1

InChI key

LFZGBNATHRHOKZ-KRWDZBQOSA-N

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Application

N-Glutaryl-L-phenylalanine p-nitroanilide has been used as a substrate to determine chymotrypsin activity.

Biochem/physiol Actions

N-Glutaryl-L-phenylalanine p-nitroanilide is useful in testing α-chymotrypsin activity.

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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Daniel Brugger et al.
The British journal of nutrition, 116(3), 425-433 (2016-05-28)
This study investigated the effects of short-term subclinical Zn deficiency on exocrine pancreatic activity and changes in digestive capacity. A total of forty-eight weaned piglets were fed ad libitum a basal diet (maize and soyabean meal) with adequate Zn supply
New properties of chymotrypsin modified by fixation with a hydrophobic molecule: hexanal.
M H Remy et al.
Annals of the New York Academy of Sciences, 434, 343-346 (1984-01-01)
S V Verevka
Ukrainskii biokhimicheskii zhurnal (1978), 68(3), 36-41 (1996-05-01)
Data on the kinetics of S2'-stimulated alpha-chymotrypsin action have been presented. It is supposed that the increase of the catalytic action of S2'-stimulated chymotrypsin occurs at all three stages of the hydrolytic process-at the enzyme-substrate complex formation, its transformation to
S Blais et al.
The Journal of biological chemistry, 268(25), 18637-18639 (1993-09-05)
The Michaelis constant of alpha-chymotrypsin, immobilized on a glutaraldehyde-activated silicate support, for N-glutaryl-L-phenylalanine-p-nitroanilide was determined and was found to be identical with that of the enzyme in solution. The influence of intraparticular diffusion was taken into account by immobilizing different
N Spreti et al.
European journal of biochemistry, 268(24), 6491-6497 (2001-12-12)
alpha-Chymotrypsin activity was tested with N-glutaryl-l-phenylalanine p-nitroanilide (GPNA) in aqueous media in the presence of synthetic surfactants, which differ in the flexibility of their bulky head groups. Superactivity can be ascribed to the presence of the tributylammonium residue on the

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