[3H]可乐定在肝细胞膜上的多个结合位点。

Multiple binding sites of [3H]clonidine on hepatic plasma membranes.

作者信息

Lacombe C, Haidamous M, Krimian R, Kouyoumdjian J C

出版信息

Gen Pharmacol. 1984;15(4):315-9. doi: 10.1016/0306-3623(84)90007-7.

Abstract

The binding of [3H]clonidine on mouse liver plasma membrane was a rapid, saturable and reversible process. It was characterized by two types of population: high affinity receptors with KD of 6.76 +/- 1.02 nM and Bmax of 106.15 +/- 24.05 fmol/mg protein, and low affinity receptors with KD of 63.66 +/- 12.85 nM and Bmax of 818.06 +/- 128.49 fmol/mg protein. Displacement of [3H]clonidine from its binding sites by various ligands indicated that alpha 1--as well as alpha 2--adrenoceptors were involved in the high affinity system. The respective participation of these two types of receptors was discussed.

摘要

[3H]可乐定与小鼠肝细胞膜的结合是一个快速、可饱和且可逆的过程。它具有两种类型的群体特征：高亲和力受体，其解离常数（KD）为6.76±1.02 nM，最大结合容量（Bmax）为106.15±24.05 fmol/mg蛋白质；低亲和力受体，其KD为63.66±12.85 nM，Bmax为818.06±128.49 fmol/mg蛋白质。各种配体将[3H]可乐定从其结合位点置换出来，表明α1以及α2肾上腺素能受体参与了高亲和力系统。讨论了这两种类型受体各自的参与情况。