[Use of Edman's method for splitting actinoidin peptides and aglycone].
Phenylthiohydantoins of amino acids isolated from actinoidine (n-oxyphenylglycine, 3-chlor-4-oxyphenylglycine, actinoidinic amino acid) were prepared. Their spectral and chromagraphic properties were studied. Splitting of the aglycone of actinoidine and the prodlcts of its incomplete acid hydrolysis (peptides Y-Phe and B-Y-Phe) was achieved with the Edman method. Parital structure of tripeptide B-Y-Phe (4NH2-group) was proposed. Tripeptide B-Y Phe constitutes about 80 per cent of the antibiotic aglycone part.
D000900:Anti-Bacterial Agents / Q000032:analysis*; D002854:Chromatography, Paper; D002855:Chromatography, Thin Layer; D006020:Glycopeptides / Q000032:analysis*; D008968:Molecular Conformation; D009842:Oligopeptides / Q000302:isolation & purification*; D010443:Peptide Chain Termination, Translational; D010446:Peptide Fragments / Q000032:analysis; D010669:Phenylthiohydantoin; D013056:Spectrophotometry, Ultraviolet; D013861:Thiocyanates; D014640:Vancomycin / Q000031:analogs & derivatives
D000900:Anti-Bacterial Agents; D006020:Glycopeptides; D009842:Oligopeptides; D010446:Peptide Fragments; D013861:Thiocyanates; D010669:Phenylthiohydantoin; C012164:actinoidins; D014640:Vancomycin
Primenenie metoda Edmana dlia rasshchepleniia peptidov i aglikona aktinoidina