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A sensitive radioimmunoassay for the lipolytic peptide B from pig pituitary glands has been developed. Antisera were raised in rabbits, which allowed a final dilution of 1:6000. Free and antibody bound [125I]peptide B could be separated by double antibody, by dextran-coated charcoal and by polyethyleneglycol. The smallest detectable amount was 0.5 ng/ml. Peptide B could be measured irregularly in porcine sera; there was crossreacting material in an extract of a total human pituitary gland, but not in human sera. The assay seems specific except for a strong cross-reaction with porcine neurophysin. There are indications that peptide B consists of neurophysin and a small lipolytically active peptide which remains to be further characterized.The isolation of lipolytic peptides from pituitary glands has been reported (Schwandt 1974) for various species. From pig pituitary glands we have iso¬ lated peptide B; its lipolytical and other metabolic effects have been described elsewhere (Schwandt 1973; Weisweiler 8c Schwandt 1975). The acidic (Ip. 4.39) peptide B from pig pituitary glands, which has a molecular weight of about 11 000, is homogenous in column chromatography and analytical acrylamidgelelectrophoresis, has only one N-terminal aminoacid (Ruschewski et al. 1973) and contains two tyrosine residues. For further studies on the physiological relevance of lipotrophic hormones and the regulation mechanisms of lipolysis we tried to set up a radioimmunoassay for the lipolytic peptide B.