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An approach to sequencing proteins by the solid-phase method combined with isolation of proteins and polypeptides by gel electrophoresis is described. Mixtures of proteins or polypeptides resulting from digests arc fractionated in the presence of dodecylsulphate in polyacrylamide gels. They are detected with Coomassic blue, eluted, selectively reacted with porous glass derivatives and sequenced in their amino-terminal regions with the aid of a new microsequencer. Alternatively they can be analysed or digested with enzymes and fingerprinted. It is a relatively rapid method of purifying proteins for sequence analysis which we have used to provide partial protein sequence data to complement DNA sequences. Nine genes, four from the sine operon of Escherichia cpli encoding the α, β, γ and ϵ subunits of ATP synthase and live for capsid proteins of bacteriophage lambda. have been identified by this method. [ABSTRACT FROM AUTHOR]