Pfister C, Dorey C, Vadot E, Mirshahi M, Deterre P, Chabre M, Faure J P
C R Acad Sci III. 1984;299(8):261-5.
In Vertebrate retinal rod outer segments, a soluble "48 K" protein binds to disk membranes upon illumination in presence of ATP or GTP (H. Kühn, Biochemistry, 17, 1978, p. 4389). Its binding to photoexcited rhodopsin implies a probable role of the "48 K" protein in the ATP dependent regulation of the photoinduced enzymatic cascade which controls the hydrolysis of cGMP. The "retinal S antigen" is also a soluble protein located in photoreceptor cells which is known to be an organ-specific auto-antigen inducing experimental autoimmune uveoretinitis. Using extracts of purified cattle and frog rod outer segments, purified bovine S antigen, and monoclonal antibodies against S antigen, we found that both proteins exhibit identical characteristics with respect to: their migration in SD S-gel electrophoresis; their binding to rod disc membranes upon illumination in presence of ATP or GTP; their immunological reactivity with monoclonal antibodies.
在脊椎动物视网膜视杆细胞的外段中，一种可溶性的“48K”蛋白在ATP或GTP存在的情况下光照时会与盘状膜结合（H.库恩，《生物化学》，第17卷，1978年，第4389页）。它与光激发的视紫红质结合意味着“48K”蛋白可能在依赖ATP的光诱导酶促级联反应调节中发挥作用，该酶促级联反应控制着cGMP的水解。“视网膜S抗原”也是一种位于光感受器细胞中的可溶性蛋白，已知它是一种器官特异性自身抗原，可诱发实验性自身免疫性葡萄膜视网膜炎。使用纯化的牛和蛙视杆细胞外段提取物、纯化的牛S抗原以及抗S抗原的单克隆抗体，我们发现这两种蛋白在以下方面表现出相同的特征：它们在SDS凝胶电泳中的迁移；在ATP或GTP存在的情况下光照时它们与视杆盘状膜的结合；它们与单克隆抗体的免疫反应性。
