![]() N-2-Naphthylalaninamide hydrochloride (1:1) structure
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Common Name | N-2-Naphthylalaninamide hydrochloride (1:1) | ||
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CAS Number | 74144-49-3 | Molecular Weight | 250.724 | |
Density | N/A | Boiling Point | 450.1ºC at 760 mmHg | |
Molecular Formula | C13H15ClN2O | Melting Point | 258-260ºC (dec.)(lit.) | |
MSDS | Chinese USA | Flash Point | 226ºC | |
Symbol |
![]() GHS08 |
Signal Word | Warning |
Simple color tests based on an alanyl peptidase reaction which differentiate Listeria monocytogenes from other Listeria species.
J. Clin. Microbiol. 35(8) , 2155-6, (1997) 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 ... |
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The identification of Listeria species.
Int. J. Food Microbiol. 38(1) , 77-81, (1997) 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 h... |
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Glycyl-L-leucine transport in the rat small intestine.
Can. J. Physiol. Pharmacol. 60(9) , 1177-84, (1982) 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... |
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Analysis of the structure of ribonuclease A in native and partially denatured states by time-resolved noradiative dynamic excitation energy transfer between site-specific extrinsic probes.
Biochemistry 34(49) , 15965-78, (1995) 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... |
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Multiple molecular forms of human alanine aminopeptidase: immunochemical properties.
Clin. Chim. Acta 107(3) , 245-56, (1980) 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 obtaine... |
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Histochemical demonstration of exopeptidases in the rat visceral yolk-sac epithelium.
Histochemistry 82(4) , 397-400, (1985) 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 studi... |
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[Changes in the aminopeptidase activity in the brain neurons of rats subjected long-term to alcoholic intoxication].
Tsitologiia 32(10) , 1006-9, (1990) A histochemical investigation was made of aminopeptidase activities using L-leucine-beta-naphthylamide and D, L-alanine-beta-naphthylamine as respective substrates in the rat's sensomotor cortex neurons during the period of ethanol withdrawal after a prolonge... |
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Purification and characterization of a Cl- -activated aminopeptidase from bovine skeletal muscle.
Biosci. Biotechnol. Biochem. 70 , 1110-1117, (2006) To elucidate the mechanisms involved in the increase in free amino acids during postmortem storage of meat, a novel aminopeptidase was purified from bovine skeletal muscle by ammonium sulfate fractionation and successive chromatographies such as DEAE-cellulos... |
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A novel mammalian high-molecular-weight aminopeptidase.
Arch. Biochem. Biophys. 344(1) , 228-34, (1997) Studies with the human lymphoma U937 cell line revealed the presence of two soluble aminopeptidase activities. Using specific antisera one of these was identified as the puromycin-specific aminopeptidase, while the other appeared to be a novel approximately 2... |
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Purification and characterization of human seminal plasma aminopeptidase.
Ital. J. Biochem. 37(3) , 148-64, (1988) 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, on... |