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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000604:Amino Acyl-tRNA Synthetases; D001226:Aspartate-tRNA Ligase; D055598:Chemical Phenomena; D002621:Chemistry; D003488:Cyanogen Bromide; D006868:Hydrolysis; D010446:Peptide Fragments / Q000032:analysis*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D014357:Trypsin; D000604:Amino Acyl-tRNA Synthetases; D001226:Aspartate-tRNA Ligase; D003488:Cyanogen Bromide