The protein-surfactant interaction was reviewed focusing the combination of bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS). The binding and removal nature of SDS to and from BSA was firstly described. The stepwise nature of the complex formation between them was discussed on the basis of capillary electrophoresis and electrophoretic light scattering data. A discussion was made on conformational changes of the protein and its fragments mainly based on circular dichroism and dynamic light scattering. Kinetic aspects of the conformational changes were also reviewed. In some cases, the interactions of BSA with other ionic surfactants were introduced to compare with the interaction with SDS. In addition, a conformational change of the protein in a reverse micelle was also introduced in order to take notice of a role of an electrostatic influence on the protein-surfactant interaction.