InChI
1S/C15H21N3O4/c16-9-5-4-8-12(15(21)22)18-13(19)10-17-14(20)11-6-2-1-3-7-11/h1-3,6-7,12H,4-5,8-10,16H2,(H,17,20)(H,18,19)(H,21,22)
SMILES string
NCCCCC(NC(=O)CNC(=O)c1ccccc1)C(O)=O
InChI key
LRCZLURYHGISRZ-UHFFFAOYSA-N
assay
≥98% (TLC)
form
powder
solubility
water: 50 mg/mL, clear, colorless
storage temp.
−20°C
Quality Level
General description
Substrate for carboxypeptidase B and carboxypeptidase N.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
L Michelutti et al.
Clinical biochemistry, 20(1), 21-29 (1987-02-01)
Creatine kinase conversion factor has been isolated from human serum and purified to electrophoretic and chromatographic homogeneity. The enzyme sequentially converts creatine kinase MM3 to MM2 and MM1 and hydrolyzes lysine and arginine from hippuryl-L-lysine and hippuryl-L-arginine. Data on molecular
Koichi Itakura et al.
Chemistry and physics of lipids, 124(2), 81-88 (2003-06-24)
2-Hydroxyheptanal (2-HH) is one of the major aldehydes derived from peroxidation of polyunsaturated fatty acids. In the present study, to obtain an insight into the contributions of 2-HH to protein modifications during lipid peroxidation, a lysine-containing dipeptide, N(alpha)-hippuryllysine (N-benzoylglycyl-L-lysine, BGL)
R J Edwards et al.
The Biochemical journal, 221(2), 465-470 (1984-07-15)
The effect of partially purified 'creatine kinase conversion factor' on rabbit muscle creatine kinase is shown to be that of a carboxypeptidase, removing the C-terminal lysine residue from both subunits. These changes fully explain the three-banded electrophoretic patterns of the
F Marceau et al.
Journal of chromatography, 266, 173-177 (1983-08-26)
A rapid and sensitive method for measuring carboxypeptidase N (CPN) activity in human plasma is described. The procedure is based on the hydrolysis of a high-specificity/low-affinity substrate, hippuryl-L-lysine, to its products hippuric acid and lysine. The substrate and product are
A A Lavras et al.
Acta physiologica latino americana, 30(4), 269-274 (1980-01-01)
Evidence is presented to suggest that kininase activity of Bothrops jararaca plasma is due to the presence of at least three distinct enzymes: a carboxypeptidase B type enzyme, similar to that found in human plasma in that its activity is
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