Skip to Content
Merck
All Photos(3)

Documents

G1135

Sigma-Aldrich

L-Glutamic acid γ-(4-nitroanilide)

γ-glutamyl transpeptidase substrate

Synonym(s):

L-γ-Glutamyl-p-nitroanilide, L-Glutamic acid 5-(4-nitroanilide)

Sign Into View Organizational & Contract Pricing
All Photos(3)

About This Item

Linear Formula:
C11H13N3O5
CAS Number:
7300-59-6
Molecular Weight:
285.25
Beilstein:
2818758
EC Number:
230-748-5
MDL number:
MFCD00036218
UNSPSC Code:
12352204
PubChem Substance ID:
24895042
NACRES:
NA.83

Assay

≥98% (HPLC)

form

powder

solubility

formic acid: 50 mg/mL, clear to slightly hazy

storage temp.

2-8°C

SMILES string

N[C@@H](CCC(=O)Nc1ccc(cc1)[N+]([O-])=O)C(O)=O

InChI

1S/C11H13N3O5/c12-9(11(16)17)5-6-10(15)13-7-1-3-8(4-2-7)14(18)19/h1-4,9H,5-6,12H2,(H,13,15)(H,16,17)/t9-/m0/s1

InChI key

WMZTYIRRBCGARG-VIFPVBQESA-N

Looking for similar products? Visit Product Comparison Guide

Substrates

Substrate for γ-glutamyl transpeptidase

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

K Abe et al.
Bioscience, biotechnology, and biochemistry, 61(10), 1621-1625 (1997-11-15)
Two isozymes of gamma-glutamyltranspeptidase, GGT-A and GGT-B, were purified to electrophoretic homogeneity from a culture broth of Bacillus subtilis TAM-4, which produces poly(gamma-glutamic acid) (PGA) de novo. GGT-A was composed of three subunits with molecular weights of 23,000 (I), 39,000
H Speisky et al.
Alcohol (Fayetteville, N.Y.), 7(4), 339-347 (1990-07-01)
The localization of gamma-glutamyl transferase (GGT) in the intact rat liver was studied by a new approach in which the chromogenic gamma-glutamyl donor substrate of GGT gamma-glutamyl-p-nitroanilide is perfused through the portal vein to yield p-nitroaniline, which is monitored spectrophotometrically.
T Friedrich et al.
European journal of biochemistry, 256(2), 297-302 (1998-10-06)
A new enzyme from Hirudo medicinalis capable of splitting gamma-glutamyl-p-nitroanilide and Glu--Lys-(N6-gamma-glutamyllysine) (isopeptidic bond between the epsilon-amino group of lysine and the gammacarboxylic group of glutamic acid) isopeptide bonds was purified. The protein was partially sequenced at the amino acid
Y Carrion et al.
Biochemical pharmacology, 45(12), 2527-2535 (1993-06-22)
The effect of thyroid hormone administration on liver glutathione (GSH) content and gamma-glutamyltransferase activity in the isolated perfused liver was studied for a period of 1-7 days in fed rats following a single dose of 0.1 mg 3,5,3'-L-triiodothyronine (T3)/kg. T3
I P Baskova et al.
Biokhimiia (Moscow, Russia), 55(4), 674-679 (1990-04-01)
The molecular mass of destabilase isolated from the medicinae leech Hirudo medicinalis was found to be equal to 12.3 kDa. A kinetic analysis of the sole presently known synthetic substrate, L-gamma-Glu-pNA, showed that the enzyme is relatively stable to heating
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service