[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]

C R Acad Sci III. 1984;299(8):261-5.
[Article in French]


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.

Publication types

  • English Abstract

MeSH terms

  • Animals
  • Antigens / metabolism*
  • Anura
  • Arrestin
  • Autoimmune Diseases / immunology
  • Cattle
  • Eye Proteins / isolation & purification*
  • Photic Stimulation
  • Photoreceptor Cells / metabolism*
  • Protein Binding
  • Retinal Pigments / metabolism*
  • Retinitis / immunology
  • Rhodopsin / metabolism*
  • Uveitis / immunology


  • Antigens
  • Arrestin
  • Eye Proteins
  • Retinal Pigments
  • Rhodopsin