Primary structure of aspartyl-tRNA synthetase from baker's yeast: tryptic and CNBr peptides

The cristallizable aspartyl-tRNA synthetase from Baker's yeast is a dimer made up of identical subunits (Mr 60,000). We report here the results of tryptic digestion and cyanogen bromide cleavage which enabled us to align two lon stretches of sequence of 106 and 111 amino acids, respectively.