Studies on the primary structure of 14 proteins from the large subunit of Escherichia coli ribosomes with an improved protein sequenator and with mass spectrometry.
Fourteen proteins from the large subunit of Escherichia coli ribosomes were analyzed in an improved sequenator. In addition to our previously described modifications of a Beckman sequenator, new valves which work free of a dead volume were constructed. By this and the previous improvements (e.g., a new vacuum system with a recorder, cool traps, automatic conversion) much better results were obtained than before. It was even possible to use (in addition to the standard methods, e.g., thin-layer chromatography and amino acid analysis) mass spectrometry without preceding gas chromatography for identification of the released PTH amino acids. Our experience with the various methods, especially mass spectrometry, is described and the techniques are compared. The results obtained by the described methods on the amino acid sequences of the 14 ribosomal proteins are summarized.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001322:Autoanalysis / Q000295:instrumentation*; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification; D002849:Chromatography, Gas; D002855:Chromatography, Thin Layer; D004926:Escherichia coli / Q000032:analysis*; D006868:Hydrolysis; D013058:Mass Spectrometry; D011487:Protein Conformation; D012270:Ribosomes / Q000032:analysis*
D000596:Amino Acids; D001426:Bacterial Proteins