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This paper describes the use of phenyl-Sepharose CL-4B as a solid-phase hydrophobic adsorbent in the purification of S-antigen from protein extracts of bovine, porcine and human retina. Chromatographic conditions were ascertained whereby the majority of contaminating proteins were bound to the adsorbent leaving S-antigen in the liquid phase. In combination with size fractionation on Ultrogel AcA, the method conveniently yielded porcine and bovine S-antigen preparations up to 100% purity. Immunogenicity of purified S-antigens was verified by induction of experimental autoimmune uveoretinitis in albino Lewis rats. The method is preparative in scale, fast in performance and yields S-antigen in high purity and antigenic potency.
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