Deuteration kinetics of tyrosine by means of fluorescence measurement.
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概要
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When tyrosine was rapidly transferred from water into deuterium oxide medium by means of a stopped-flow device, a time-dependent change in the fluorescence intensity at 305 nm (excited at 275 nm) has been observed. The rate constant (<I>k</I><SUB>e</SUB>) was found to be 116 s<SUP>−1</SUP> at pH 5.8 and 14 °C. This <I>k</I><SUB>e</SUB> value has been attributed to the rate constant of the O<SUP>1</SUP>H→O<SUP>2</SUP>H reaction of the phenolic OH group, on the basis of similar fluorescence examinations on phenol, anisole, glycyl-L-tyrosine, and <I>N</I><SUP>α</SUP>-acetyl-<I>N</I>-methyl-L-tyrosinamide as well as on the basis of a stopped-flow ultraviolet absorption study of tyrosine. The stopped-flow fluorometry has been applied to a study of tyrosine residues in yeast 3-phosphoglycerate kinase.
- 公益社団法人 日本化学会の論文
著者
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Nakanishi Mamoru
Faculty Of Pharmaceutical Science University Of Tokyo
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Tsuboi Masamichi
Faculty of Pharmaceutical Sciences, The University of Tokyo
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Tsuboi Masamichi
Faculty of Parmaceutical Sciences, The University of Tokyo
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