Barrios V, Fernandez Iriarte M C, Morcillo E, Prieto J C, Arilla E
Departamento de Bioquímica, Universidad de Alcalá de Henares, Madrid, Spain.
Regul Pept. 1987 Nov;19(3-4):149-59. doi: 10.1016/0167-0115(87)90272-2.
Somatostatin binding sites have been demonstrated in the cytosolic fraction of guinea-pig lung. Binding of 125I-Tyr11-somatostatin was dependent on time and temperature, saturable, reversible and highly specific. Under equilibrium condition, i.e. 60 min at 25 degrees C, native somatostatin inhibited tracer binding in a dose-dependent manner. Two types of somatostatin binding sites were defined by Scatchard analysis: a small population with a high affinity (Kd = 23.4 nM) and a large population with a low affinity (Kd = 253.5 nM) for somatostatin. The biphasic nature of the dissociation process confirmed the heterogeneity of somatostatin binding sites. Apart from somatostatin, no peptide (1 microM) tested influenced the binding of 125I-Tyr11-somatostatin. The present data represent the first analysis of somatostatin binding sites in lung.
已在豚鼠肺的胞质部分证实了生长抑素结合位点。125I-Tyr11-生长抑素的结合依赖于时间和温度，具有饱和性、可逆性且高度特异。在平衡条件下，即在25℃孵育60分钟，天然生长抑素以剂量依赖方式抑制示踪剂结合。通过Scatchard分析确定了两种类型的生长抑素结合位点：对生长抑素具有高亲和力（Kd = 23.4 nM）的小群体和低亲和力（Kd = 253.5 nM）的大群体。解离过程的双相性质证实了生长抑素结合位点的异质性。除生长抑素外，所测试的任何肽（1 microM）均不影响125I-Tyr11-生长抑素的结合。目前的数据代表了对肺中生长抑素结合位点的首次分析。
