Kalinina S N, Etingof R N
Biokhimiia. 1984 Apr;49(4):679-85.
A scheme of immunization of rabbits with partially purified GTP-binding proteins isolated from ox retinal photoreceptor membranes has been developed. Using double radial immunodiffusion, it was shown that rabbit antiserum interacts with the GTP-binding proteins of the retinal phosphoreceptor membranes of ox, pig and frog. The antibodies interaction with the GTP-binding proteins of ox retinal rod outer segments was followed by immunoelectrophoresis as well as by elimination of the activating effect of the non-hydrolyzable derivative of GTP, guanyl-5'-yl-imidodiphosphate on cyclic nucleotide phosphodiesterase in illuminated photoreceptor membranes and in their extracts. A similar effect was exerted by immunoglobulins from immunized animals on the enzyme activation by NaF. Purified immunoglobulins type G did not practically interact with the GTP-binding proteins of the photoreceptor membranes.
已制定了用从牛视网膜光感受器膜中分离出的部分纯化的GTP结合蛋白免疫家兔的方案。使用双向放射免疫扩散法表明，兔抗血清可与牛、猪和蛙的视网膜磷光感受器膜的GTP结合蛋白相互作用。通过免疫电泳以及消除不可水解的GTP衍生物鸟苷-5'-基-亚氨基二磷酸对光照的光感受器膜及其提取物中环核苷酸磷酸二酯酶的激活作用，来跟踪抗体与牛视网膜视杆外段的GTP结合蛋白的相互作用。免疫动物的免疫球蛋白对氟化钠激活该酶也有类似作用。纯化的G型免疫球蛋白实际上不与光感受器膜的GTP结合蛋白相互作用。
