A GTPASE-ACCELERATING FACTOR FOR TRANSDUCIN, DISTINCT FROM ITS EFFECTOR CGMP PHOSPHODIESTERASE, IN ROD OUTER SEGMENT MEMBRANES
A GTPASE-ACCELERATING FACTOR FOR TRANSDUCIN, DISTINCT FROM ITS EFFECTOR CGMP PHOSPHODIESTERASE, IN ROD OUTER SEGMENT MEMBRANES
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DOI：
10.1016/0896-6273(93)90123-9
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发表时间：
1993-11-01
期刊：
影响因子：
16.2
通讯作者：
WENSEL, TG
中科院分区：
文献类型：
--
作者：
ANGLESON, JK;WENSEL, TG
发现光感受器G蛋白转导素（G（talpha））水解GTP的动力学与其效应物cGMP磷酸二酯酶（PDE）的失活相同，但在稀释的视杆外节（ROS）悬浮液中太慢（数十秒），无法解释光响应的亚秒级恢复。提高ROS膜的浓度增加了GTP水解和PDE失活的速率平行多达6倍。Holo-PDE及其γ亚基对GT3动力学的影响较弱，
Hydrolysis of GTP by the photoreceptor G protein transducin (G(talpha)) was found to occur with kinetics identical to the inactivation of its effector cGMP phosphodiesterase (PDE), but was too slow (tens of seconds) in dilute rod outer segment (ROS) suspensions to account for subsecond recovery of the light response. Raising the concentration of ROS membranes increased the rates of GTP hydrolysis and PDE inactivation in parallel as much as 6-fold. Holo-PDE and its gamma subunit had weak effects on GTPase kinetics (