ABSTRACT
Many of the techniques used in the formation of liposomes or liposome-protein recombinants involve initial solubilization of the lipid or lipid-protein mixture in detergents or organic solvents. Care must be taken to reduce residual levels of detergents or solvents to low levels in order to ensure both accuracy and uniformity of experimental results. The most important considerations in the removal of detergents from liposomes are the critical micelle concentration and the aggregation number. In a typical liposome preparation made by removing ionic detergents by dialysis, from 2 to 6 mol of detergent are required to solubilize 1 mol of phospholipid although some investigators have formed liposomes successfully with ratios as low as 0.5. However, one of the important applications of liposome formation from detergent solution involves protein reconstitution, and experience has shown that many membrane proteins will not retain their structural integrity when extracted by ionic detergents as compared to nonionic detergents.
