InChI key
JWHURRLUBVMKOT-HNNXBMFYSA-N
InChI
1S/C16H20N2O/c1-11(2)9-15(17)16(19)18-14-8-7-12-5-3-4-6-13(12)10-14/h3-8,10-11,15H,9,17H2,1-2H3,(H,18,19)/t15-/m0/s1
SMILES string
CC(C)C[C@H](N)C(=O)Nc1ccc2ccccc2c1
assay
≥98% (TLC)
form
powder
solubility
H2O: insoluble
storage temp.
−20°C
Quality Level
General description
Substrate for aminopeptidase M
Application
L-Leucine β-naphthylamide has been used as a substrate:
- to measure the activity of aminopeptidase in Escherichia coli
- to evaluate the enzyme activity of cathepsin H from rabbit skeletal muscles
- in the proteolytic assay of L-Leucine aminopeptidase
Substrate for leucine aminopeptidase determination in colorimetric and histochemical procedures.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Analysis Note
Very low free β-naphthylamine.
Nikou Hesari et al.
Enzyme and microbial technology, 83, 22-28 (2016-01-19)
There remains a need for rapid, specific and sensitive assays for the detection of bacterial indicators for water quality monitoring. In this study, a strategy for rapid detection of Escherichia coli in drinking water has been developed. This strategy is
Mohamad Elzein et al.
Journal of environmental science and health. Part A, Toxic/hazardous substances & environmental engineering, 48(8), 925-932 (2013-03-15)
The objective of the study was to identify the enzymatic-biochemical (enz-bio) signatures of Escherichia coli and Salmonella for rapid detection of these bacteria in drinking water biofilms. The relative potency of lipophilic, glucosidic, and proteolytic activities in biofilms containing single
H Yokozeki et al.
The American journal of physiology, 252(6 Pt 2), R1119-R1129 (1987-06-01)
Attempts were made to purify and characterize cysteine proteinases in human eccrine sweat and further clarify their origin. Benzoyl-DL-arginine-beta-naphthylamide (BANA) and L-leucine beta-naphthylamide (LeuNA) hydrolases in thermally induced sweat were sequentially purified by Sephacryl S-200 chromatography and chromatofocusing, which yielded
F Alba et al.
Life sciences, 43(11), 935-939 (1988-01-01)
Levels of soluble aminopeptidase (AP), measured as arylamidase activity using L-Leucine-2-Naphthylamide (Leu-2-NA) as substrate, were determined in the soluble fraction of eleven zones of rat brain. Results showed that AP activity is asymmetrically distributed in frontal cortex and hypothalamus with
R Alidina et al.
Experimental and molecular pathology, 49(1), 118-127 (1988-08-01)
Squamous cell carcinomas (SCC) were experimentally produced in hairless mouse skin, and cysteine protease and its inhibitor were simultaneously purified from extracts of 1 g of tissue of SCC and normal skin. Activity of cysteine proteinases, Mr greater than 50,000
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