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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)

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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

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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)

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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
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
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
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