The sequence determination of a protein in a micro scale: the sequence analysis of ribosomal protein L34 of Escherichia coli.
The complete amino acid sequence of ribosomal protein L34 has been established by improved micro techniques with 3 mg of the lyophilized protein. The protein was digested with trypsin, thermolysin and chymotrypsin and the resulting peptides were isolated from fingerprints performed on cellulose thin-layer plates. The amino acid sequences of the peptides were determined by the combined micro dansyl-Edman technique using 5 - 10 nmol per sample. Aspartic acid and glutamic acid were distinguished from their amides by use of the color reaction of ninhydrin with the respective amino acid phenylthiohydantoins.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002855:Chromatography, Thin Layer; D002918:Chymotrypsin; D003619:Dansyl Compounds; D004926:Escherichia coli / Q000032:analysis*; D006868:Hydrolysis; D008832:Microchemistry; D010446:Peptide Fragments / Q000032:analysis; D012269:Ribosomal Proteins; D014357:Trypsin
D001426:Bacterial Proteins; D003619:Dansyl Compounds; D010446:Peptide Fragments; D012269:Ribosomal Proteins; D002918:Chymotrypsin; D014357:Trypsin