Evidence for somatostatin binding sites in rabbit kidney.
Specific binding sites for somatostatin have been identified in cytosolic fraction of rabbit kidney (cortex and outer medulla) using 125I-Tyr11-somatostatin. The binding was saturable and reversible, as well as time and temperature dependent. Optimal pH for binding was observed at about 7.4. Scatchard plots were compatible with the existence of two classes of binding sites: a first class with a high affinity (Kd = 40 nM) and a low binding capacity (2.0 pmol somatostatin/mg protein) and a second class with a low affinity (Kd = 222 nM) and a high binding capacity (114.3 pmol somatostatin/mg protein). Vasoactive intestinal peptide, neurotensin, substance P, Leu-enkephalin and vasopressin had practically no effect on somatostatin binding. The properties of these binding sites strongly support the concept that somatostatin could behave as a regulatory peptide on the rabbit kidney.
Roca
B
B
Arilla
E
E
Prieto
J C
JC
D000818:Animals; D001667:Binding, Competitive; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000032:analysis*; D007700:Kinetics; D008297:Male; D010455:Peptides / Q000494:pharmacology; D011485:Protein Binding; D011817:Rabbits; D011956:Receptors, Cell Surface / Q000032:analysis*; D017481:Receptors, Somatostatin; D013004:Somatostatin / Q000031:analogs & derivatives* / Q000378:metabolism; D013696:Temperature
D010455:Peptides; D011956:Receptors, Cell Surface; D017481:Receptors, Somatostatin; D013004:Somatostatin; C032367:somatostatin, Tyr(11)-