Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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3',5'-Cyclic-GMP Phosphodiesterases / metabolism*
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Animals
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Antigens* / isolation & purification
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Arrestin
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Autoimmune Diseases / etiology
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Cattle
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Eye Proteins / immunology
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Eye Proteins / isolation & purification
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Eye Proteins / pharmacology
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Light
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Molecular Weight
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Photoreceptor Cells / enzymology*
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Rats
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Retina / analysis
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Retina / immunology*
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Rod Cell Outer Segment / analysis
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Rod Cell Outer Segment / immunology
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Uveitis / etiology
Substances
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Antigens
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Arrestin
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Eye Proteins
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3',5'-Cyclic-GMP Phosphodiesterases