Micropolarity of sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles prepared in supercritical ethane and near-critical propane

Conformational Changes of Bovine Serum A

Conformational Changes of Bovine Serum Albumin in an Aqueous Solution of Sodium Bis(2-ethylhexyl) Sulfosuccinate and in the Reverse Micelle of the Same Surfactant

✍ Kunio Takeda; Kazumasa Harada; Kouji Yamaguchi; Yoshiko Moriyama 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 284 KB

The helicity of bovine serum albumin (BSA) decreased both in the reverse micelle of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) and in the aqueous solution of the same surfactant (the saturated binding amount to the protein was \(70 \mathrm{~mol} / \mathrm{mol}\) ). In both cases, the final helici