[The mechanism of binding of sodium dodecyl sulfate by lysozyme]

It has been shown that the mechanism of complex formation changes at variation of the detergent concentration. At low concentrations the complex is stabilized, mainly, by hydrophobic interactions. The boded molecules are immobilized inside the globules. At concentrations close to critical micellization concentration only some of the molecules take part in such strong binding, while the rest form weak bonds and may be removed by gel filtrations. Presumably in this case electrostatic interactions dominate in binding processes. At concentrations exceeding critical micellization concentration complex formation is controlled by electrostatic association of protein with aggregates of the detergent's molecules, stabilized, like micelles by hydrophobic forces. The complex is unstable.