March 1987
Volume 28, Issue 3
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Articles  |   March 1987
Immunoaffinity purification of S-antigen using monoclonal antibodies to different antigenic sites.
Investigative Ophthalmology & Visual Science March 1987, Vol.28, 604-607. doi:
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      J P Banga, S Suleyman, E Kasp, E Brown, F LeRoy, M Sanders, D Dumonde; Immunoaffinity purification of S-antigen using monoclonal antibodies to different antigenic sites.. Invest. Ophthalmol. Vis. Sci. 1987;28(3):604-607.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Retinal S-antigen (S-ag) was purified by monoclonal antibody (MoAb) immunoaffinity chromatography from soluble protein extracts of bovine and human retina. Purification of S-ag was readily achieved by affinity chromatography using four different MoAb-Sepharose 4B columns. The four antibody columns gave different recoveries with material of comparable enrichment with greater than 95% purity as judged by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The use of two different MoAbs covalently bound to Sepharose 4B and known to be directed to disparate, spacially distant epitopes on S-ag led to at least a twofold increase in recovery, with the aforementioned purity. Immunoaffinity purified S-ag retained its serological and uveitogenic properties. The high recovery of S-ag associated with this one-step procedure is preferable to conventional preparatory techniques, and enables high antigen recovery when tissue availability is limited (eg human retina).

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