The amino acid sequence of the N-terminal two-thirds of a trout high-mobility-group protein, HMG-T, has been determined as a continuous sequence of 174 residues out of a total for the whole molecule of 260 residues. When this sequence was compared with published sequences of long cyanogen bromide-derived peptides from the analogous calf-thymus proteins, HMG-1 and -2 (Walker et al. , 1979), there was strong homology, with 60-70% identity of corresponding amino acid residues in the three proteins, the majority in lengthy identical runs. However, a discrepancy in the position of a highly acidic run of aspartic and glutamic residues suggests this region may not lie within the main polypeptide chain but may represent a separate chain or possibly a branched structure. VSports手机版.