A2503
DL-Alanine β-naphthylamide hydrochloride
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About This Item
Fórmula lineal:
CH3CH(NH2)CONHC10H7·HCl
Número de CAS:
Peso molecular:
250.72
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.83
Productos recomendados
assay
≥98% (TLC)
form
powder
mp
258-260 °C (dec.) (lit.)
solubility
ethanol: 50 mg/mL, clear to slightly hazy
storage temp.
2-8°C
SMILES string
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
InChI key
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.
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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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