Publikationsdatum:
1985-05-17
Beschreibung:
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〉
Schlagwort(e):
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
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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