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  • Title: [Identification of the so-called 48 K protein that interacts with illuminated rhodopsin in retinal rods, and the retinal S antigen, inductor of experimental autoimmune uveoretinitis].
    Author: Pfister C, Dorey C, Vadot E, Mirshahi M, Deterre P, Chabre M, Faure JP.
    Journal: C R Acad Sci III; 1984; 299(8):261-5. PubMed ID: 6439387.
    Abstract:
    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.
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