Assay
≥98% (TLC)
Quality Level
form
powder
solubility
water: 50 mg/mL, clear, colorless
storage temp.
−20°C
SMILES string
NCCCCC(NC(=O)CNC(=O)c1ccccc1)C(O)=O
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)
InChI key
LRCZLURYHGISRZ-UHFFFAOYSA-N
Substrates
Substrate for carboxypeptidase B and carboxypeptidase N.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Journal of agricultural and food chemistry, 56(7), 2522-2527 (2008-03-06)
The reaction of the Nalpha-hippuryllysine (BzGK) with fructose was investigated in two model systems to obtain an insight in fructose-induced modification of lysine in bakery products. After BzGK and fructose had been heated in a buffered low-moisture model system (80
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)
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
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
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
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