5-(2-Aminoethyl)dithio-2-nitrobenzoate as a more base-stable alternative to Ellman's reagent.
作者： Jinge Zhu , Ilirian Dhimitruka , Dehua Pei
DOI: 10.1021/OL048404+
关键词: Base (chemistry) 、 Ellman's reagent 、 Chemistry 、 Kinetics 、 5-(2-aminoethyl)dithio-2-nitrobenzoate 、 Reagent 、 Medicinal chemistry 、 Extramural 、 Thiol 、 Enzymatic Assays 、 Organic chemistry
摘要: [reaction: see text] 5-(2-Aminoethyl)dithio-2-nitrobenzoate (ADNB) reacts with free thiols kinetics similar to those of Ellman's reagent but has dramatically improved stability under alkaline conditions, making it an excellent alternative for the quantitation thiol contents and enzymatic assays basic pH conditions.
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Heinz Faulstich, Daniela Heintz, [34] Reversible introduction of thiol compounds into proteins by use of activated mixed disulfides Methods in Enzymology. ,vol. 251, pp. 357- 366 ,(1995) , 10.1016/0076-6879(95)51139-3
Peter W. Riddles, Robert L. Blakeley, Burt Zerner, [8] Reassessment of Ellman's reagent Enzyme Structure Part I. ,vol. 91, pp. 49- 60 ,(1983) , 10.1016/S0076-6879(83)91010-8
Susan M. Aitken, Jack F. Kirsch, Kinetics of the Yeast Cystathionine β-Synthase Forward and Reverse Reactions: Continuous Assays and the Equilibrium Constant for the Reaction† Biochemistry. ,vol. 42, pp. 571- 578 ,(2003) , 10.1021/BI026681N
George L. Ellman, K.Diane Courtney, Valentino Andres, Robert M. Featherstone, A new and rapid colorimetric determination of acetylcholinesterase activity Biochemical Pharmacology. ,vol. 7, pp. 88- 95 ,(1961) , 10.1016/0006-2952(61)90145-9
Hao Zhang, Min Le, Gary E. Means, A Kinetic Approach to Characterize the Electrostatic Environments of Thiol Groups in Proteins Bioorganic Chemistry. ,vol. 26, pp. 356- 364 ,(1998) , 10.1006/BIOO.1998.1112
M. G. Surette, M. B. Miller, B. L. Bassler, Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: A new family of genes responsible for autoinducer production Proceedings of the National Academy of Sciences of the United States of America. ,vol. 96, pp. 1639- 1644 ,(1999) , 10.1073/PNAS.96.4.1639
Ying Zhou, Xiao-Chuan Guo, Tian Yi, Tadashi Yoshimoto, Dehua Pei, Two Continuous Spectrophotometric Assays for Methionine Aminopeptidase Analytical Biochemistry. ,vol. 280, pp. 159- 165 ,(2000) , 10.1006/ABIO.2000.4513
H. Faulstich, P. Tews, D. Heintz, Determination and Derivatization of Protein Thiols by n-Octyldithionitrobenzoic Acid Analytical Biochemistry. ,vol. 208, pp. 357- 362 ,(1993) , 10.1006/ABIO.1993.1061
Peter Eyer, Franz Worek, Daniela Kiderlen, Goran Sinko, Anita Stuglin, Vera Simeon-Rudolf, Elsa Reiner, Molar absorption coefficients for the reduced Ellman reagent: reassessment. Analytical Biochemistry. ,vol. 312, pp. 224- 227 ,(2003) , 10.1016/S0003-2697(02)00506-7
Karen S. Brown, William D. Kingsbury, Norman M. Hall, George L. Dunn, Charles Gilvarg, Determination of carboxypeptidase A using N-acetyl-phenylalanyl-3-thiaphenylalanine as substrate: application to a direct serum assay. Analytical Biochemistry. ,vol. 161, pp. 219- 225 ,(1987) , 10.1016/0003-2697(87)90674-9