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Published October 1, 1983 | public
Journal Article Open

Avian lens spectrin: subunit composition compared with erythrocyte and brain spectrin


Chicken lens spectrin is composed predominantly of equimolar amounts of two polypeptides with solubility properties similar, but not identical, to erythrocyte spectrin. The larger polypeptide, Mr 240,000 (lens alpha- spectrin), co-migrates with erythrocyte and brain alpha-spectrin on one- and two-dimensional SDS polyacrylamide gels and cross-reacts with antibodies specific for chicken erythrocyte alpha-spectrin; the smaller polypeptide, Mr 235,000 (lens gamma-spectrin), co-migrates with brain gamma-spectrin and does not cross-react with either the alpha-spectrin antibodies specific for chicken erythrocyte beta-spectrin. Minor amounts of polypeptides antigenically related to erythrocyte beta- spectrin with a greater electrophoretic mobility than lens gamma- spectrin are also detected in lens. The equimolar ratio of lens alpha- and gamma-spectrin is invariantly maintained during the extraction of lens plasma membranes under different conditions, or after immunoprecipitation of whole extracts of lens with erythrocyte alpha- spectrin antibodies. Two-dimensional peptide mapping reveals that whereas alpha-spectrins from chicken erythrocytes, brain, and lens are highly homologous, the gamma-spectrins, although related, have some cell-type-specific peptides and are substantially different from erythrocyte beta-spectrin. Thus, the expression of cell-type-specific gamma- and beta-spectrins may be the basis for the assembly of a spectrin-plasma membrane complex whose molecular composition is tailored to the functional requirements of the particular cell-type.

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Copyright © 1983 by The Rockefeller University Press. RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode. Received for publication 15 July 1983. We thank Dr. R.T. Moon for his helpful comments on the manuscript. This work was supported by grants from the National Institutes of Health (NIH), the National Science Foundation, and the Muscular Dystrophy Association of America, and by a Biomedical Research Support Grant to the Division of Biology, California Institute of Technology. W.J. Nelson was also supported by an international fellowship from the Cancer Research Campaign awarded by the International Union Against Cancer and B.L. Granger by a postdoctoral fellowship from the Muscular Dystrophy Association of America. E. Lazarides is the recipient of a Research Career Development Award from the NIH.


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