Kinetics of the conformational change and subunit dissociation of aldolase.

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概要

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• The kinetics of acid denaturation of muscle aldolase were examined by stopped-flow fluorescence and stopped-flow light scattering measurements. The denaturation reaction was found to consist of three distinguishable steps—step I with fluorescence increase only, step II with both fluorescence increase and light scattering decrease, and step III with fluorescence decrease alone. Circular dichroism and sedimentation equilibrium measurements were also made at different pH's in the course of the acid denaturation. It was concluded that in the acid denaturation of this enzyme a rearrangement of the secondary or tertiary structures takes place rapidly (4 s<SUP>−1</SUP> at 21.5 °C and at pH 3.4), and then the subunit dissociation occurs more slowly (0.04 s<SUP>−1</SUP> at 21.5 °C and at pH 3.4), with further conformational change. The subunit dissociation was found to be caused by two H<SUP>+</SUP> per tetramer.

• 公益社団法人 日本化学会の論文

著者

• Nakanishi Mamoru

  Faculty of Pharmaceutical Sciences, The University of Tokyo

関連論文

• Kinetics of the conformational change and subunit dissociation of aldolase.

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