L1635
L-Leucine β-naphthylamide
别名:
L-Leucine-2-naphthylamide
一般描述
Substrate for aminopeptidase M
应用
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.
包装
Bottomless glass bottle. Contents are inside inserted fused cone.
分析说明
Very low free β-naphthylamine.
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
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
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
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
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
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