Renaturation of Myoglobin Denatured by Sodium Dodecyl Sulfate by Removal of Dodecyl Sulfate Ions Bound to the Protein Using Sodium Cholate.

The secondary and tertiary structures of myoglobin were disrupted by sodium dodecyl sulfate (SDS) but were hardly affected by the bile salt, sodium cholate (NaCho). This disruption was induced by the binding of dodecyl sulfate (DS) ions to the protein. In this study, the removal of DS ions bound to the protein was attempted using NaCho. The extent of removal of DS ions was estimated by the restoration of the secondary and tertiary structures of the protein disrupted by SDS. The secondary structural change was followed by monitoring mean residue ellipticity at 222 nm, [θ]