Bovine retinal S-antigen was prepared using gel filtration chromatography followed by DEAE A-50 or QAE A-50 anion-exchange chromatography. The final purification was performed using immunoadsorbents made from polymerized polyvalent antiserum (rabbit) to bovine serum components. The purity of the antigen was confirmed by polyacryl-amide gel electrophoresis, double diffusion according to Ouchterlony, immunoblotting and by producing monospecific antiserum to the retinal S-antigen. Both S-antigen preparations (DEAE and QAE) proved to be highly uveitogenic, causing experimental allergic uveitis in guinea pigs within 14 days of immunization. DEAE separated the antigen into three protein peaks but QAE only into one distinct protein peak. All these protein peaks were S-antigen-active and the yield was about the same using both separation systems. After optimizing the purification for bovine retinas, human retinal S-antigen was also prepared.

Keywords:
Retinal S-antigen, Purification, Experimental autoimmune uveitis, Immunoadsorbance
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© 1989 S. Karger AG, Basel
1989
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