Abstract
The ability of chaotropic agents to solubilize the regularly structured (RS) protein from the outer membrane of Aquaspirillum serpens VHA was determined by electron microscopy and sodium dodecyl sulfate – polyacrylamide gel electrophoresis. The RS protein was not solubilized by cationic substitution, low pH, sodium deoxycholate, or some nonionic detergents. Some outer membrane proteins were solubilized along with the RS protein by octyl-β-D-glucopyranoside, sodium N-lauroyl sarcosinate, and zwitterionic detergents. Selective solubilization of the RS protein was achieved with lithium 3,5-diiodosalicylate.
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