The selective solubilization of pig stratum corneum (SC) by the nonionic surfactant octyl glucoside (OG) was investigated. The use of OG concentrations lower than its critical micelle concentration (CMC) led to a progressive solubilization of SC membranes whereas OG concentrations higher than its CMC provided an increase in its solubilizing power. In these conditions, some amino acids building the SC keratinocyte envelopes and bound to the lipids by covalent bonds were extracted. TEM revealed during and after surfactant incubation the type of structures formed which may be correlated with the formation of some colloid association between SC components and OG. The OG may be considered as a more suitable solubilizing agent than solvents to obtain more specific and selective solubilization of SC components without a protein denaturing effect.