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Science 17 May 1985:
Vol. 228. no. 4701, pp. 891 - 893
DOI: 10.1126/science.2988124
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Articles

Science, Vol 228, Issue 4701, 891-893
Copyright © 1985 by American Association for the Advancement of Science

articles

Retinal S antigen identified as the 48K protein regulating light-dependent phosphodiesterase in rods

C Pfister, M Chabre, J Plouet, VV Tuyen, Y De Kozak, JP Faure, and H Kuhn

Retinal S antigen chromatographically purified from whole retina, induces experimental autoimmune uveoretinitis in laboratory animals. The 48K protein, a soluble protein found in rod outer segments, is purified through its specific binding to photoexcited rhodopsin and is involved in the quenching of light-induced guanosine 3',5'-monophosphate-phosphodiesterase activity. Biochemical, immunological, functional, and pathological tests showed that retinal S antigen and the 48K protein are identical.


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