The complete amino acid sequences of ribosomal proteins L17, L27, and S9 from Bacillus stearothermophilus

Abstract
The complete primary structures of proteins L17, L27 and S9 extracted from the B. stearothermophilus ribosomes with 1 M NaCl and purified to homogeneity by column chromatography were determined. The amino acid sequences of these proteins are compared to those of the homologous ribosomal proteins from Escherichia coli. The number of identical amino acid residues between the homologous proteins lies between 33-55%.