Abstract
STUDIES of the interactions between detergent and protein solutions by a wide variety of techniques have provided useful information on the types of binding involved in these systems1 and on the denaturation and re-orientation of protein molecules2. In particular, the system bovine serum albumin – sodium dodecyl sulphate has been extensively investigated by electrophoresis, sedimentation and viscosity methods by Putnam and co-workers3, and the heats of interaction for this system have recently been measured in this Laboratory by a direct calorimetric method4. The present communication deals with the effect of salt on the turbidity of bovine serum albumin – sodium dodecyl sulphate solutions.
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