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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

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P M Verhoeff et al.
Clinica chimica acta; international journal of clinical chemistry, 175(2), 129-134 (1988-07-15)
In this paper we compare the measurement of catalytic activity concentrations of gamma-glutamyltransferase with the non-carboxylated and the carboxylated substrate in preparations of different origin. Fresh human sera, commercial test sera and preparations of gamma-glutamyltransferase purified from human liver, porcine
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
S Finney et al.
The Biochemical journal, 324 ( Pt 3), 797-805 (1997-06-15)
1. Crude salivary gland extract of the giant Amazon leech, Haementeria ghilianii, contains an inhibitor of plasma factor XIIIa. 2. The inhibitory agent was purified to homogeneity by anion-exchange, cation-exchange, gel-filtration and reverse-phase chromatography to yield a single band on
Gololobov MYu et al.
The Biochemical journal, 304 ( Pt 3), 869-876 (1994-12-15)
Acyl-transfer catalysed by gamma-glutamyltranspeptidase from bovine kidney was studied using gamma-L- and gamma-D-Glu-p-nitroanilide as the donor and GlyGly as the acceptor. The transfer of the gamma-Glu group to GlyGly was shown to be accompanied by transfer of the gamma-Glu group
L Dvoráková et al.
General physiology and biophysics, 15(5), 403-413 (1996-10-01)
The initial rate kinetics of rat kidney gamma-glutamyl transpeptidase were measured using L-gamma-glutamyl-p-nitroanilide and glycyl-glycine as the donor and the acceptor substrate, respectively. Experimental data were fitted with the initial rate equation, and the obtained results indicated that: (1) Michaelis
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