An antiserum was raised against the peptide PE-11 whose sequence is present in the chromogranin B molecule. The antiserum reacts only with the free C-terminal end of this peptide. PE-11 immunoreactivity in brain was characterized by molecular size exclusion high performance liquid chromatography. Only the free peptide and a N-terminally elongated peptide were detected, indicating that proteolytic processing of chromogranin B in brain is quite extensive. In immunohistochemistry PE-11 immunoreactivity was found in varicosities, fibres and perikarya throughout the brain. Strong staining was detected in the shell sector of the nucleus accumbens, in the lateral septum, in subregions of the extended amygdala, in some areas of the hippocampus and of the hypothalamus, in the locus coeruleus, in the Purkinje cells of the cerebellum and in the dorsal horn of the spinal cord. Our results, which demonstrate significant processing of chromogranin B in brain and its widespread distribution, can be taken as an indication that chromogranin B represents a precursor of peptides with functional relevance for this organ.