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A2503
DL-Alanin-2-naphthylamid -hydrochlorid
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About This Item
Lineare Formel:
CH3CH(NH2)CONHC10H7·HCl
CAS-Nummer:
Molekulargewicht:
250.72
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
eCl@ss:
32160406
PubChem Substanz-ID:
NACRES:
NA.83
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Assay
≥98% (TLC)
Form
powder
mp (Schmelzpunkt)
258-260 °C (dec.) (lit.)
Löslichkeit
ethanol: 50 mg/mL, clear to slightly hazy
Lagertemp.
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
InChIKey
WNLRRMRLNYQNOZ-UHFFFAOYSA-N
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Anwendung
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
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
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
D R Buckler et al.
Biochemistry, 34(49), 15965-15978 (1995-12-12)
Formation of local structure and overall chain dimensions in the 124-residue, four-disulfide protein bovine pancreatic ribonuclease A (RNase A) under conditions favoring either the native or partially folded states have been studied by nonradiative excitation energy transfer measurements. Three RNase
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