Specific somatostatin-binding to cytosol of bovine gallbladder mucosa.

The binding of somatostatin was studied in the cytosolic fraction of bovine gallbladder mucosa. The binding reaction depended on time, temperature and pH, and was reversible, saturable and specific. Stoichiometric data suggested the presence of two classes of binding sites: a class with high affinity (Kd = 23.6 nM) and low capacity (3.7 pmol somatostatin/mg protein) and a class with low affinity (Kd = 284.6 nm) and high capacity (85.0 pmol somatostatin/mg protein) at 37 degrees C and pH 7.4. The binding sites were highly specific for somatostatin since peptides such as [Leu]enkephalin, neurotensin, vasoactive intestinal peptide and substance P showed practically no effect upon somatostatin binding. The presence of somatostatin-binding sites in the cytosolic fraction of gallbladder mucosa, together with the known occurrence of somatostatin nerve endings in the gallbladder strongly suggests that this peptide may be involved in the physiology and physiopathology of gallbladder mucosa.