Retinal S antigen identified as the 48K protein regulating light-dependent phosphodiesterase in rods.
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.
Pfister
C
C
Chabre
M
M
Plouet
J
J
Tuyen
V V
VV
De Kozak
Y
Y
Faure
J P
JP
Kühn
H
H
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D000941:Antigens / Q000302:isolation & purification; D019393:Arrestin; D001327:Autoimmune Diseases / Q000209:etiology; D002417:Cattle; D005136:Eye Proteins / Q000276:immunology / Q000302:isolation & purification / Q000494:pharmacology; D008027:Light; D008970:Molecular Weight; D010786:Photoreceptor Cells / Q000201:enzymology*; D051381:Rats; D012160:Retina / Q000032:analysis / Q000276:immunology*; D012374:Rod Cell Outer Segment / Q000032:analysis / Q000276:immunology; D014605:Uveitis / Q000209:etiology
D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D015106:3',5'-Cyclic-GMP Phosphodiesterases