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H2508

Sigma-Aldrich

Hippuryl-Arg

carboxypeptidase substrate, chromogenic, ≥98% (TLC), powder

Sinonimo/i:

N-Benzoyl-Gly-Arg

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About This Item

Formula empirica (notazione di Hill):
C15H21N5O4
Numero CAS:
744-46-7
Peso molecolare:
335.36
Numero CE:
212-015-1
Numero MDL:
MFCD00055706
Codice UNSPSC:
12352204
ID PubChem:
24895502
NACRES:
NA.32

product name

Hippuryl-Arg, carboxypeptidase substrate

Saggio

≥98% (TLC)

Forma fisica

powder

Solubilità

water: 50 mg/mL, clear, colorless to faintly yellow

Temperatura di conservazione

−20°C

Stringa SMILE

NC(=N)NCCC[C@H](NC(=O)CNC(=O)c1ccccc1)C(O)=O

InChI

1S/C15H21N5O4/c16-15(17)18-8-4-7-11(14(23)24)20-12(21)9-19-13(22)10-5-2-1-3-6-10/h1-3,5-6,11H,4,7-9H2,(H,19,22)(H,20,21)(H,23,24)(H4,16,17,18)/t11-/m0/s1
GFLCPYUSPYXNBV-NSHDSACASA-N

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Categorie correlate

Applicazioni

Hippuryl-Arg has been used as a substrate for:
  • aminopeptidase from Trogoderma granarium
  • exopeptidase from Bactrocera oleae Gmelin, midgut of Plagiodera versicolora
  • carboxypeptidase from Pichia pastoris

Azioni biochim/fisiol

Hippuryl-Arg is a synthetic substrate for carboxypeptidase B, and aminopeptidase. The enzyme carboxypeptidase acts on C terminal of arginine and lysine.

Substrati

Substrate for carboxypeptidase B and carboxypeptidase N.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

Certificati d'analisi (COA)

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Proteolytic activity in Plagiodera versicolora Laicharting (Coleoptera: Chrysomelidae): Characterization of digestive proteases and effect of host plants
Zibaee A and Hajizadeh J
Journal of Asia-Pacific Entomology, 16(3), 329-334 (2013)
Hidefumi Komura et al.
Microbiology and immunology, 46(2), 115-117 (2002-04-10)
Carboxypeptidases (CP) in plasma and sera serve as regulators of anaphylatoxins such as C3a and C5a. The activity of CP can be measured by determining hippuric acid after cleavage of the small synthetic substrate hippuryl-L-arginine. Although a colorimetric assay is
Yu-Hong Liu et al.
FEBS letters, 580(22), 5137-5142 (2006-09-12)
This work reports the use of electrospray mass spectrometry for studying the conformational dynamics of enzymes by amide hydrogen/deuterium exchange (HDX) measurements. A rapid-mixing quench-flow approach allows comparisons to be made between the HDX kinetics of free enzymes with those
S Appelros et al.
Biological chemistry, 379(7), 893-898 (1998-08-15)
Recent developments in the treatment of acute pancreatitis have focused on the importance of early determination of the severity of an attack. Measuring levels of activation peptides from pancreatic proenzymes seems to be one way to predict severity. Levels of
H Schweisfurth et al.
Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie, 21(10), 605-609 (1983-10-01)
Kininase I (carboxypeptidase N; EC 3.4.17.3) consists of carboxypeptidase N1 (CN1) and carboxypeptidase N2 (CN2); these two enzymes can be differentiated by their activities towards hippuryl-L-arginine and hippuryl-L-lysine, respectively. A spectrophotometric assay for both carboxypeptidases in human serum is described
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