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  • 1
    Publication Date: 1985-05-17
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfister, C -- Chabre, M -- Plouet, J -- Tuyen, V V -- De Kozak, Y -- Faure, J P -- Kuhn, H -- New York, N.Y. -- Science. 1985 May 17;228(4701):891-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988124" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Animals ; *Antigens/isolation & purification ; Arrestin ; Autoimmune Diseases/etiology ; Cattle ; Eye Proteins/immunology/isolation & purification/pharmacology ; Light ; Molecular Weight ; Photoreceptor Cells/*enzymology ; Rats ; Retina/analysis/*immunology ; Rod Cell Outer Segment/analysis/immunology ; Uveitis/etiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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