August 1965
Volume 4, Issue 4
Articles  |   August 1965
Immunochemistry of the Lens With Special Reference to Phylogeny
Author Affiliations
    Department of Ophthalmology Research, Columbia University, College of Physicians and Surgeons, New York, N. Y.
    Department of Ophthalmology Research, Columbia University, College of Physicians and Surgeons, New York, N. Y.
Investigative Ophthalmology & Visual Science August 1965, Vol.4, 539-559. doi:
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      WLADYSLAW MANSKI, SEYMOUR P. HALBERT; Immunochemistry of the Lens With Special Reference to Phylogeny. Invest. Ophthalmol. Vis. Sci. 1965;4(4):539-559.

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

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Lenses from all vertebrate classes were used for preparing antisera in rabbits. By immunoelectrophoresis, 9 to 10 precipitin lines were found in all homologous reactions. The number of lens components shared by different vertebrates depended on their relative position in the evolutionary scale. The absorption of any given antilens serum with lenses from another class removed antibodies against lens components shared by both with species lower in the evolutionary scale. These results indicate that some lens components developed at an earlier evolutionary stage were transferred to higher species, which retained them throughout all or part of further evolutionary transformations. Appropriately absorbed antilens sera can be thus used for tracing the sequence of appearance of each lens component in human or other lenses. In attempts to isolate phylogenetically different lens components, continuous flow electrophoresis, column chromatography, isolectric and ethanol precipitation were used. Almost all the bovine lens fractions analyzed immunologically proved to be mixtures. Components with the same immunological specificity occurred in a heterogeneity of forms, which differed in solubility, electrophoretic and chromatographic properties. These data point to the necessity of immunochemical analysis as an accessory procedure. The possible role of protein interactions, aging, and genetic variations as causes of difficulty in the separation of individual lens proteins was briefly discussed. Additional investigations described the similarities and differences of antibodies to rabbit lens obtained by injecting (a) rabbit lens into rabbits, (b) other vertebrate lenses into rabbits, and (c) rabbit lens into other vertebrates, e.g., ducks.


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