Light-induced binding of guanosinetriphosphatase to bovine photoreceptor membranes: effect of limited proteolysis of the membranes.
Light-induced binding of guanosinetriphosphatase to bovine photoreceptor membranes: effect of limited proteolysis of the membranes.
复制标题
光诱导的鸟苷三磷酸酶与牛光感受器膜的结合：膜的有限蛋白水解作用。
DOI：
10.1021/bi00512a007
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Hargrave,PA
中科院分区：
文献类型：
--
作者：
Kühn,H;Hargrave,PA
Hermann Kiihn*和Paul A. Hargrave*摘要：比较了棒状细胞鸟苷三磷酸酶（GTPase）在不同离子强度和光照条件下与棒状细胞盘膜和经有限蛋白水解修饰的盘膜的结合。以牛棒外段为原料，用热裂解素酶解制备了两种不同的改性膜。(短期消化从视紫红质羧基端去除12个氨基酸[Hargrave， P. A. & Fong, s . l .(1977)]。Supramol。结构[6,99]，长期消化导致进一步裂解产生两个大的非共价相关膜结合片段[Pober， JS, & Stryer， L.(1975) J. Mol. Biol. 95,477]。将含有GTPase和其他可溶性蛋白的纯化棒外段提取物添加到不同的圆盘膜制剂中，并在黑暗和光照下测量与膜的结合。在低离子强度下，GTPase在黑暗中可溶，但在光照下变成膜结合；这种光诱导结合既发生在短期消化的盘上，也发生在未消化的对照盘上，这表明紫红质羧基末端的12个氨基酸不参与这种光诱导结合反应。然而，长期消化的磁盘表现出大大降低的光诱导容量
Hermann Kiihn* and Paul A. Hargrave* abstract: The binding of rod cell guanosinetriphosphatase (GTPase) to rod cell disk membranes, and to disk membranes which have been modified by limited proteolysis, has been compared under different conditions of ionic strength and illumination. Disk membranes purifiedfrom bovine rod outer segments were digested with fhermolysin to produce two different modified preparations.(Short-term digestion removes 12 amino acids from rhodopsin’s carboxyl terminus [Hargrave, P. A., & Fong, S.-L.(1977)/. Supramol. Struct. 6, 99], Long-term digestion leads to further cleavage (s) producing two large noncovalently associated membrane-bound fragments [Pober, JS, & Stryer, L.(1975) J. Mol. Biol. 95, 477].) The extract frompurified rod outer segments, containing the GTPase and other soluble proteins, Was added to the different disk membrane preparations, and binding to the membranes was measured in the dark and following exposure to light. At low ionic strength the GTPase was soluble in the dark but became membrane bound upon illumination; this light-induced binding occurred to short term digested disks as well as to undigested control disks, indicating that the 12 amino acids from rhodopsin’s carboxyl terminus are not involved in this light-induced binding reaction. Long term digested disks, however, exhibited a greatly diminished light-induced capacity