title: [The purification and analysis of S-antigen in rabbit retina].
abstract: OBJECTIVE
  S-antigen from rabbit retina was isolated and purified to investigate the immune mechanisms of experimental autoimmune uveoretinitis (EAU) and lay a foundation for its experimental treatment.
  
  
  METHODS
  Two-step ion exchange chromatography was used for the purification of S-antigen and it was analyzed.
  
  
  RESULTS
  The analytical studies show that the molecular weight of the purified S-antigen is 55,000, its isoelectric point is 6.40, and non-polar amino acid constitutes a relatively large proportion in its amino acids. Scanning tunnel electron microscope was used to investigate the configuration of S-antigen. It is elliptic globe-like. The purified S-antigen successfully induced the model of EAU.
  
  
  CONCLUSIONS
  S-antigen purified by two-step ion exchange chromatography can be used for its own analytical studies and induction of EAU model.
authors: Beijing Institute of Ophthalmology.
authors: X
authors: X
authors: Sun
authors: C
authors: C
authors: Zhang
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000941:Antigens / Q000737:chemistry / Q000302:isolation & purification*; D019393:Arrestin; D001327:Autoimmune Diseases / Q000209:etiology; D002852:Chromatography, Ion Exchange; D005136:Eye Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008297:Male; D011817:Rabbits; D051381:Rats; D017208:Rats, Wistar; D012160:Retina / Q000737:chemistry*; D012173:Retinitis / Q000209:etiology; D014605:Uveitis / Q000209:etiology
chemical_list: D000596:Amino Acids; D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins