Abstract
Solubilization of the human erythrocyte membrane by 7 detergents is described. Components released into the supernatant or retained in the residue were identified by sodium dodecyl sulfate/polyacrylamide-gel electrophoresis. Two non-ionic detergents exhibiting little UV absorption were more efficient than UV-absorbing Triton X-100. Evidence is presented of an interchange between protein PAS [periodic acid Schiff] 1 and protein PAS 2.