Jizheng Dang, Hongbo Liu, Xiaolan Yang, Yi Zhang, Yanling Xie, Yuanli Li, Jun Pu, Juan Liao, Yonghua Yuan, Fei Liao
Unit for Analytical Probes and Protein Biotechnology, Key Laboratory of Medical Laboratory Diagnostics of the Education Ministry, College of Laboratory Medicine, Chongqing Medical University, Chongqing 400016, China.
Bioorganic & medicinal chemistry letters 2013 Feb 1At pH from 5.5 to 7.6, absorptivity of 4-nitro-1-naphthol at 450 nm is over 2.1-fold of that of para-nitrophenol at 405 nm and over 9.6-fold of that of ortho-nitrophenol at 415 nm. On 4-nitro-1-naphthyl-β-D-galactopyranoside at pH 7.4, catalytic efficiency of Escherichia coli β-D-galactosidase is 3-fold of that on para-nitrophenyl-β-D-galactopyranoside and about 40% of that on ortho-nitrophenyl-β-D-galactopyranoside, and produces a lower quantification limit of penicillin G by enzyme-linked-immunoabsorbent-assay. Hence, 4-nitro-1-naphthol is favorable to prepare chromogenic substrates of hydrolytic enzymes of neutral or slightly acidic optimum pH. Copyright © 2012 Elsevier Ltd. All rights reserved.
Jizheng Dang, Hongbo Liu, Xiaolan Yang, Yi Zhang, Yanling Xie, Yuanli Li, Jun Pu, Juan Liao, Yonghua Yuan, Fei Liao. Chromogenic substrate from 4-nitro-1-naphthol for hydrolytic enzyme of neutral or slightly acidic optimum pH: 4-nitro-1-naphthyl-β-D-galactopyranoside as an example. Bioorganic & medicinal chemistry letters. 2013 Feb 1;23(3):646-9
PMID: 23267768
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