  The solubilizing power of various nonionic and zwitterionic detergents as
membrane protein solubilizers for two-dimensional electrophoresis was
investigated. Human red blood cell ghosts and Arabidopsis thaliana leaf
membrane proteins were used as model systems. Efficient detergents could be
found in each class, i.e. with oligooxyethylene, sugar or sulfobetaine polar
heads. Among the commercially available nonionic detergents, dodecyl maltoside
and decaethylene glycol mono hexadecyl ether proved most efficient. They
complement the more classical sulfobetaine detergents to widen the scope of
useful detergents for the solubilization of membrane proteins in proteomics.
