[Amino acid sequence of various peptides of tryptophanyl-tRNA-synthetase from bovine pancreas].

Method of isolation of the bovine pancreas tryptophanyl-tRNA synthetase is improved and a protein with greater than or equal to 99% purity, according to PAGE-SDS, is obtained. The pure enzyme is digested with clostripain and the hydrolysate is separated by FPLC anion-exchange chromatography followed by reversed phase HPLC. Amino acid sequences of 6 individual peptides, including C-terminal one, were determined by the automated Edman degradation. A peptide is also revealed which is encoded with the low degeneracy.