Abstract
A mixture of integral membrane proteins from Sendai virus was used as a model to study the effect of various detergents and organic solvent on the purification by size-exclusion high-performance liquid chromatography (HPLC) on two tandemly linked Superose-6 columns. The best separations were obtained with either 0.1% sodium dodecyl sulphate, 0.05% sarkosyl or 0.1% lauryldimethylamineoxide in the eluent. In addition, the effect of the eluent on the immunological activity as a measure of intact structure was studied. A considerable part of the protein structure remained intact after HPLC and was able to react with antibodies directed against the intact virus proteins.
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