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   <subfield code="a">Mesotocin Binding to Receptors in Hen Kidney Plasma Membranes</subfield>
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   <subfield code="c">[TETSUYA TAKAHASHI, MITSUO KAWASHIMA, A TADASHI YASUOKA, MICHIHARU KAMIYOSHI, KATUHIDE TANAKA]</subfield>
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   <subfield code="a">Radioligand assays were performed to demonstrate the presence of a receptor for mesotocin (MT) in the membrane fractions of the kidney of the hen. Specific [125I]MT bindings were decreased by the presence of Mg2+ and Ca2+, increased by the presence of EDTA, increased during the first 4 h of incubation and then reached a plateau, and increased with the increase in the protein concentration from 2.5 to 20 μg. The membrane fraction showed binding specificity to [125I]MT. The Scatchard plot revealed a curvilinear profile that indicated the presence of two classes of binding sites: a high affinity site and a low affinity site. The equilibrium dissociation constant was 0.08 ± 0.01 nM (χ̄ ± SEM; n = 5) in the high affinity site and 0.87 ± 0.08 nM (n = 5) in the low affinity site. The maximum binding capacity of the high and low affinity sites was 42 ± 4 and 129 ± 6 fmol/mg protein, respectively. The results suggest the presence of two distinct MT receptors in the kidney of the hen.</subfield>
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