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Merck

G1135

Sigma-Aldrich

L-谷氨酸 γ-(4-硝基苯胺)

γ-glutamyl transpeptidase substrate

别名:

L-γ-谷氨酰--硝基苯胺, L-谷氨酸5-(4-硝基苯胺)

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About This Item

线性分子式:
C11H13N3O5
CAS号:
分子量:
285.25
Beilstein:
2818758
EC號碼:
MDL號碼:
分類程式碼代碼:
12352204
PubChem物質ID:
NACRES:
NA.83

化驗

≥98% (HPLC)

形狀

powder

溶解度

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

儲存溫度

2-8°C

SMILES 字串

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 密鑰

WMZTYIRRBCGARG-VIFPVBQESA-N

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基底

用作γ-谷氨酰转肽酶的底物

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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The reaction of oxidized and reduced glutathione (with some amino-acids) and L-gamma-glutamyl p-nitroanilide with sheep kidney tissue homogenate. An examination of the reaction products by paper chromatography.
P C Nicholas et al.
Biochemical Society transactions, 19(1), 50S-50S (1991-02-01)
Long-Liu Lin et al.
Applied microbiology and biotechnology, 73(1), 103-112 (2006-07-20)
A truncated gene from Bacillus lichenifromis ATCC 27811 encoding a recombinant gamma-glutamyltranspeptidase (BLrGGT) was cloned into pQE-30 to generate pQE-BLGGT, and the overexpressed enzyme was purified from the crude extract of IPTG-induced E. coli M15 (pQE-BLGGT) to homogeneity by nickel-chelate
M Moriguchi et al.
Archives of microbiology, 144(1), 15-19 (1986-02-01)
Three gamma-glutamyltranspeptidase (enzymes I, II and III) were partially purified from the cell free extracts of the cultured mycelia of Morchella esculenta Fr. The molecular masses of enzymes were 155,000 (I), 219,000 (II) and 102,000 (III). All of them catalyzed
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
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

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