Isolation and solubilization of cellular membrane proteins from bacteria.

Membrane proteins are rarely identified in two-dimensional electrophoretic (2-DE) proteomics maps. This is because of low abundance, poor solubility, and inherent hydrophobicity. In this study, membrane preparations from the Gram-positive bacterium Streptococcus mutans were isolated from protoplasts and by mechanical grinding. Membrane proteins were extracted using a mixture of trifluroethanol and chloroform, solubilized using highly chaotropic buffer containing ASB-14 and Triton X-100 and subjected to two-dimensional gel electrophoresis.