The production and characteristics of a compound in Proteus vulgaris G cultures which was capable of inhibiting Vibrio parahaemolyticus and other food-borne pathogens was investigated. Production was influenced by medium composition, pH and temperature but not by the extent of aeration. The compound was most inhibitory at the optimum temperature for growth of V. parahaemolyticus. The inhibitor was most stable at pH 7.0 and inhibition occurred even after heating at 70 degrees C for 30 min and after autoclaving. Ultrafiltration showed that the inhibitor had a molecular weight less than 1000. Thin layer chromatography of filtrates and subsequent peptidase digestion indicated that it was at least in part a peptide. The inhibitor purified by Sephadex G-15 gel filtration had a calculated molecular weight of 731 and contained only six amino acids.