Abstract
The terminal amino acid residues of crystalline Japanese-radish peroxidase a were in-vestigated. No N-terminal amino acid was found in this enzyme by the fluorodinitrobenzene and the phenylisothiocyanate methods, while the C-terminus of this enzyme was occupied by serine, which was found by the carboxypeptidase digestion and the hydrazinolysis methods. These results suggest that this enzyme has only a single peptide chain and its N-terminal group must be blocked.