For dental plaque organisms such as Streptococcus sanguis, the ecological importance of the ability to utilize arginine as an energy source has been established in previous studies. The present investigation was undertaken to determine the ability of a strain of S. sanguis to process unsubstituted arginine-containing peptides. The organism was grown under glucose-limited conditions in a chemically defined medium, and peptide was added to washed, resting cells in a pH-stat at pH 7.0. Filtrates taken at appropriate time intervals were assayed for peptide, free amino acids, and metabolites. Irrespective of the position of the arginine residue, all peptides tested were attacked, although those that possessed a C-terminal arginine (including a tetrapeptide) were processed at a faster rate than were those in which arginine was N terminal. However, C-terminal arginine was cleaved only slowly from a peptide containing 24 residues. In each case, most of the released arginine was converted to ornithine via the arginine deiminase pathway. Such peptidase activities appeared to occur at or near the cell surface and were probably constitutive. It was found that the organism grew in chemically defined medium containing arginine that was present solely in the form of a tripeptide, and also that a strain of S. mutans possessed only a limited ability to attack arginine-containing peptides and was unable to utilize the released arginine.