Abstract
B. subtilis membrane proteins were separated by reverse phase chromatography using a simple solvent system of acetonitrile/water. The isolated proteins were further characterized by a ‘MS-FIT’ peptide mass fingerprinting program. The experimental scheme for separation and identification of membrane proteins could also be modified to detect protein-protein interactions. The method has been proven useful for rapid isolation, purification, and characterization of hydrophobic membrane proteins.

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