Bernstein K J, Verosky M, Triner L
Anesth Analg. 1985 May;64(5):531-7.
Halothane, in a number of tissues, alters the activity of adenylate cyclase, the enzyme that catalyzes the formation of cyclic 3',5'-adenosine monophosphate, an important intracellular regulator. The present studies demonstrate that in rat liver whole homogenates, basal and glucagon-stimulated adenylate cyclase activity is increased by halothane. In isolated rat liver membranes, halothane does not increase basal activity and it decreases activity stimulated by glucagon. Suspension of membranes in the cytosol fraction restores the halothane-induced increase of basal and glucagon-stimulated activity. When cytosol denatured by trypsin or heat was used, the halothane-induced increase in glucagon-stimulated activity was lost, but the increase of basal activity was still observed. Suspension of membranes in albumin solution restored the effect of halothane on basal activity only. These results suggest that presence of heat-labile proteins in the cytosol fraction that modulate the halothane interaction with rat liver adenylate cyclase.
氟烷在许多组织中会改变腺苷酸环化酶的活性，该酶催化环化3',5'-单磷酸腺苷的形成，后者是一种重要的细胞内调节因子。目前的研究表明，在大鼠肝脏全匀浆中，氟烷会增加基础状态下以及胰高血糖素刺激后的腺苷酸环化酶活性。在分离的大鼠肝细胞膜中，氟烷不会增加基础活性，反而会降低胰高血糖素刺激后的活性。将膜悬浮于胞质溶胶组分中可恢复氟烷诱导的基础活性及胰高血糖素刺激后活性的增加。当使用经胰蛋白酶或加热变性的胞质溶胶时，氟烷诱导的胰高血糖素刺激后活性的增加消失，但仍可观察到基础活性的增加。将膜悬浮于白蛋白溶液中仅恢复了氟烷对基础活性的影响。这些结果表明，胞质溶胶组分中存在热不稳定蛋白，它们可调节氟烷与大鼠肝脏腺苷酸环化酶的相互作用。
