Static and kinetic studies of the interaction of tryptophan with fluorescein mercury(II) acetate by fluorescence and absorption spectrophotometry and by fluorescence stopped-flow method.
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概要
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Fluorescein mercury(II) acetate (FMA) was found to combine with tryptophan (Trp) to form the FMA–Trp complex. The interaction was interpreted in terms of a reversible single-step binding mechanism. The dissociation constant of the complex estimated kinetically by means of the stopped-flow method using the forward and backward rate constants was in good agreement with that obtained by the static method. From comparison with several derivatives of tryptophan, it was found that the protonated amino group and the indole moiety of tryptophan are essential for the complex formation.
- 公益社団法人 日本化学会の論文
著者
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OHNISHI Masatake
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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HIROMI Keitaro
Department of Food Science & Technology, Faculty of Agriculture, Kyoto University
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Ohnishi Masatake
Department of Food Science and Technology, Kyoto University
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Taniguchi Michio
Department of Food Science and Technology, Kyoto University
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