Abstract
Abstract A single relaxation was found in the system of sodium dodecyl sulfate and bovine serum albumin using a pressure-jump method with conductivity detection. The relaxation was observed in the concentration range of the surfactant below the critical micelle concentration. The relaxation time becomes fast with the stepwise formation of a complex between them and finally attains values compatible with those in the system of the pure surfactant micelle. This suggests a correlation of the relaxation phenomena with the partial breakdown and reformation of the complex. The similarity of the complex to the surfactant micelle was discussed on the basis of the kinetic aspects of the interaction of the surfactant with the protein.
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