title: [The purification of bovine IRBP and its uveitogenic action].
abstract: The interphotoreceptor retinoid-binding protein, IRBP, shuttles the retinoid between photoreceptor cells and the pigment epithelium. It also induces experimental autoimmune uveoretinitis (EAU). The authors first purified IRBP in China by Con A Sepharose affinity chromatography in conjunction with the purification of bovine retinal S-antigen by ion-exchange chromatography. EAU was successfully induced by injection of emulsified IRBP 50 micrograms with Freund's complete adjuvant into the footpad of Lewis rats. It was characterized by panophthalmia with severe damage to the posterior retina, and lymphocytes predominated the inflammatory infiltration that included mononuclear and polymorphonuclear cells.
authors.affiliation: Zhongshan Ophthalmic Center, Sun Yat-sen University of Medical Sciences, Guangzhou.
authors.forename: P Z
authors.initials: PZ
authors.lastname: Yang
mesh_terms: D000818:Animals; D005136:Eye Proteins / Q000302:isolation & purification*; D005620:Freund's Adjuvant; D008297:Male; D010202:Panophthalmitis / Q000139:chemically induced; D051381:Rats; D011917:Rats, Inbred Lew; D012177:Retinol-Binding Proteins / Q000302:isolation & purification*; D000099214:Retinol-Binding Proteins, Interstitial
chemical_list: D005136:Eye Proteins; D005620:Freund's Adjuvant; D012177:Retinol-Binding Proteins; D000099214:Retinol-Binding Proteins, Interstitial