June 1989
Volume 30, Issue 6
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Articles  |   June 1989
Immunoreactivity and cross-reactivity of human and bovine retinal S-antigen.
Author Affiliations
  • G Doekes
    Department of Ophthalmo-Immunology, The Netherlands Ophthalmic Research Institute, Amsterdam.
  • M J Gerritsen
    Department of Ophthalmo-Immunology, The Netherlands Ophthalmic Research Institute, Amsterdam.
  • A Kijlstra
    Department of Ophthalmo-Immunology, The Netherlands Ophthalmic Research Institute, Amsterdam.
Investigative Ophthalmology & Visual Science June 1989, Vol.30, 1169-1173. doi:
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    • Get Citation

      G Doekes, M J Gerritsen, A Kijlstra; Immunoreactivity and cross-reactivity of human and bovine retinal S-antigen.. Invest. Ophthalmol. Vis. Sci. 1989;30(6):1169-1173.

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      © 2016 Association for Research in Vision and Ophthalmology.

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Abstract

The reactions of human and bovine retinal S-antigen (S-ag) with polyclonal rabbit antibodies were compared in ELISA, immunoblotting and inhibition ELISA. Titrations in ELISA with plastic-adsorbed S-ags revealed that the great majority (70-100%) of human S-ag epitopes and anti-human S-ag antibodies were cross-reactive. In contrast, the cross-reactivity of bovine S-ag (25%) and anti-bovine S-ag antibodies (15-20%) indicated an important contribution of species-specific epitopes to the antigenicity of bovine S-ag. Immunoblotting of S-ag fragments after treatment with chymotrypsin confirmed these differences and also demonstrated different chymotrypsin-induced cleavage patterns of human and bovine S-ag. Thus, in assays involving partial denaturation and/or degradation of the antigens, human S-ag showed little, and bovine S-ag a marked species-specific immunoreactivity. In inhibition ELISA however, in which S-ags in solution could be studied, species-specific reactions strongly predominated for both S-ags. Anti-human S-ag and anti-bovine S-ag antibodies could be absorbed with nM concentrations of fluid phase human and bovine S-ag, respectively, whereas in both cases the cross-reacting antigen had no detectable inhibitory potential. The epitopic structures of human and bovine S-ag in solution may thus be largely different.

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