G1135
L-Glutamic acid γ-(4-nitroanilide)
γ-glutamyl transpeptidase substrate
동의어(들):
L-γ-Glutamyl-p-nitroanilide, L-Glutamic acid 5-(4-nitroanilide)
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모든 사진(3)
About This Item
Linear Formula:
C11H13N3O5
CAS Number:
Molecular Weight:
285.25
Beilstein:
2818758
EC Number:
MDL number:
UNSPSC 코드:
12352204
PubChem Substance ID:
NACRES:
NA.83
추천 제품
분석
≥98% (HPLC)
형태
powder
solubility
formic acid: 50 mg/mL, clear to slightly hazy
저장 온도
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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기질
Substrate for γ-glutamyl transpeptidase
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
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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