The history of immunology of lens proteins goes back to Uhlenhuth,1 who 55 years ago showed by precipitation tests the organ specificity of some of the lens components. This was verified later by Burky, Woods, and Woodhall.2 They found that mainly the so-called α-crystallin was organspecific. Recently fractionation of lens proteins was improved by François, Rabaey, Wieme, and Kaminski.3,4 Using Cohn's technique with alcohol precipitation in the cold3 and paper, as well as agar gel electrophoresis,4 they were able to produce as many as eight different fractions. Rao5 used agar precipitin tests and found six components in bovine lens with rabbit antisera. Halbert and co-workers,6,7 by means of gel diffusion technique, found up to five different lens antigens with homologous rabbit antilens sera. Further experiments were performed with several heterologous lens antisera in rabbits. The cross reactions among vertebrate lenses were found to
WITMER RH. Immunoelectrophoresis of Cataractous Lenses. AMA Arch Ophthalmol. 1959;61(5):738–744. doi:10.1001/archopht.1959.00940090740010
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