title: The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus.
abstract: The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.
mesh_terms: D000595:Amino Acid Sequence; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D004926:Escherichia coli / Q000032:analysis; D001411:Geobacillus stearothermophilus / Q000032:analysis*; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D013045:Species Specificity; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D012269:Ribosomal Proteins; D002918:Chymotrypsin; D014357:Trypsin; D010434:Pepsin A; D003488:Cyanogen Bromide