Purification and characterization of 30-S ribosomal proteins from Bacillus stearothermophilus.
Twenty-three proteins were identified by two-dimensional eletrophoresis on polyacrylamide-gel slabs in the 30-S ribosomal subunit of Bacillus stearothermophilus strain 799. They were designated as B-S1 through B-S21, B-Sa and B-Sb and purified on carboxymethyl-cellulose and Sephadex G100 in the presence of 6 M urea. Their molecular weight was estimated by dodecyl-sulfate-gel electrophoresis and their amino acid composition was determined after acid hydrolysis. Results obtained for the individual proteins were essentially similar to those for Escherichia coli 30-S proteins with some characteristic differences.
D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000032:analysis*; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000032:analysis; D006868:Hydrolysis; D008623:Mercaptoethanol; D008970:Molecular Weight; D012270:Ribosomes / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate
D000596:Amino Acids; D001426:Bacterial Proteins; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol