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Key Documents

A2503

Sigma-Aldrich

DL-Alanine β-naphthylamide hydrochloride

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About This Item

Formule linéaire :
CH3CH(NH2)CONHC10H7·HCl
Numéro CAS:
Poids moléculaire :
250.72
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160406
ID de substance PubChem :
Nomenclature NACRES :
NA.83

Pureté

≥98% (TLC)

Forme

powder

Pf

258-260 °C (dec.) (lit.)

Solubilité

ethanol: 50 mg/mL, clear to slightly hazy

Température de stockage

2-8°C

Chaîne SMILES 

Cl.CC(N)C(=O)Nc1ccc2ccccc2c1

InChI

1S/C13H14N2O.ClH/c1-9(14)13(16)15-12-7-6-10-4-2-3-5-11(10)8-12;/h2-9H,14H2,1H3,(H,15,16);1H

Clé InChI

WNLRRMRLNYQNOZ-UHFFFAOYSA-N

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Application

DL-alanine β-naphthylamide (DLABN) has been used as a substrate to treat Listeria in the hydrolysis test to compare methods for the identification of Listeria species. It has been used as a substrate in the hydrolysis of DLABN to differentiate Listeria monocytogenes from other Listeria species.

Pictogrammes

Health hazard

Mention d'avertissement

Warning

Mentions de danger

Conseils de prudence

Classification des risques

Carc. 2

Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type P3 (EN 143) respirator cartridges


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Consulter la Bibliothèque de documents

W Sidorowicz et al.
Clinica chimica acta; international journal of clinical chemistry, 107(3), 245-256 (1980-11-06)
Human pancreas, kidney, and liver alanine aminopeptidases have similar if not identical antigenic determinants even though these three isoenzymes have distinctly different electrophoretic mobilities. Single precipitin lines without spur formation were obtained for all three enzymes with antisera obtained from
S K Nag Das et al.
The Italian journal of biochemistry, 37(3), 148-164 (1988-05-01)
A 50.4-fold purification of aminopeptidase is achieved by alcohol precipitation, DEAE-cellulose, CM-cellulose and finally Sephadex G-200 chromatography. On polyacrylamide gel electrophoresis of the purified enzyme after molecular sieving on Sephadex G-200, only one band was obtained, suggesting that the enzyme
C I Cheeseman et al.
Canadian journal of physiology and pharmacology, 60(9), 1177-1184 (1982-09-01)
The uptake of the peptide glycyl-L-leucine across the brush border of the rat small intestinal enterocyte was studied using everted rings. The transfer of leucine from the dipeptide into the enterocyte was greater than the glycine uptake from glycyl-L-leucine. This
A G Clark et al.
Journal of clinical microbiology, 35(8), 2155-2156 (1997-08-01)
The hydrolysis of DL-alanine-beta-naphthylamide and D-alanine-p-nitroanilide for identification of Listeria spp. has been studied with 227 cultures. All species of Listeria, except L. monocytogenes, hydrolyzed these substrates. The reactions were detected by simple chromogenic reactions and could substitute for the
P Kugler et al.
Histochemistry, 82(4), 397-400 (1985-01-01)
The localization of exopeptidase activities was demonstrated histochemically (by simultaneous azo coupling) on the visceral endoderm of whole unfixed yolk sacs of rats (12.5-18.5 days of gestation). For comparison, the topochemistry of exopeptidases was studied by conventional section histochemistry of

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