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About This Item
Linear Formula:
CH3CH(NH2)CONHC10H7·HCl
CAS Number:
Molecular Weight:
250.72
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.83
Recommended Products
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.[1] It has been used as a substrate in the hydrolysis of DLABN to differentiate Listeria monocytogenes from other Listeria species.[2]
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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
J McLauchlin
International journal of food microbiology, 38(1), 77-81 (1997-08-19)
The purpose of this study was to compare methods for the identification of Listeria species. Three hundred and fifty cultures representing the six species of Listeria were tested using conventional sugar fermentation and haemolytic reactions, as well as the hydrolysis
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
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
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