Purification of ribosomal proteins from Escherichia coli by cation exchange and reversed phase FPLC.

A complex mixture of 21 proteins from the 30S ribosomal subunit of Escherichia coli was fractionated on a cation-exchanger, then further separated on a C8 reversed-phase column. A set of 14 proteins were purified to homogeneity. The same protein mixture was also analysed on a C8 RPC column using a triethylamine phosphate (TEAP, pH2.2)/acetonitrile or a trifluoroacetic acid/acetonitrile solvent system which gave 11 and 8 purified proteins, respectively. Altogether, 16 out of 21 proteins from the 30S ribosomal subunit were purified.