title: The primary structure of initiation factor IF3 from Bacillus stearothermophilus.
abstract: The complete amino acid sequence of the initiation factor IF3 from Bacillus stearothermophilus has been elucidated. This was achieved by splitting the protein with trypsin, Staphylococcus protease or cyanogen bromide. The amino acid sequence was determined by manual Edman degradation, using the DABITC/PITC double-coupling method. The IF3 molecule contains 171 amino acids and has an Mr of 19 677. The sequence was compared to the homologous molecule from Escherichia coli; about 50% of the amino acid residues were found to be identical.
mesh_terms: D000595:Amino Acid Sequence; D003488:Cyanogen Bromide; D001411:Geobacillus stearothermophilus / Q000235:genetics*; D008836:Micrococcal Nuclease; D010446:Peptide Fragments / Q000032:analysis; D010448:Peptide Initiation Factors / Q000302:isolation & purification*; D039665:Prokaryotic Initiation Factor-3; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D014357:Trypsin
chemical_list: D010446:Peptide Fragments; D010448:Peptide Initiation Factors; D039665:Prokaryotic Initiation Factor-3; D012269:Ribosomal Proteins; D008836:Micrococcal Nuclease; D014357:Trypsin; D003488:Cyanogen Bromide