Specific receptors for glucagon and for glucagon-like peptide-1 (GLP-1) (7-36)amide have been found in solubilized human adipose membranes. The 50% inhibition dose of the corresponding unlabeled peptide was near to their physiological levels [ID50, 0.5 nmol/L for glucagon and 1.0 nmol/L for GLP-1(7-36)amide;]. In both cases, the presence of high affinity receptors was evident [Kd, 0.5 and 0.7 nmol/L for glucagon and GLP-1(7-36)amide, respectively]; the high affinity maximal binding capacity for GLP-1(7-36)amide was higher than that for glucagon (893 and 117 fmol/mg solubilized fat membranes, respectively). Glucagon at 10(-6) mol/L did not compete with the [125I]GLP-1(7-36)amide binding, nor did GLP-1(7-36)amide (10(-6) mol/L) compete with that of [125I]glucagon. The relative abundance of GLP-1(7-36)amide receptors in human adipose tissue is further support for a direct and probably important action of this peptide in the metabolism of the fat cell.