A2503
DL -丙氨酸 β-萘胺 盐酸盐
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线性分子式:
CH3CH(NH2)CONHC10H7·HCl
化学文摘社编号:
分子量:
250.72
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352204
NACRES:
NA.83
EC Number:
277-736-6
MDL number:
InChI key
WNLRRMRLNYQNOZ-UHFFFAOYSA-N
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
SMILES string
Cl.CC(N)C(=O)Nc1ccc2ccccc2c1
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
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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.
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
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
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
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
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
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