Radiation-Induced Structural Changes in Human Erythrocyte Membrane Proteins Revealed by Sodium Dodecyl Sulfate/Polyacrylamide Gel Electrophoresis

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Abstract
The effect of X-irradiation on the major proteins of human erythrocyte membranes was investigated with respect to a difference in radiosensitivity. The electrophoretic patterns on sodium dodecyl sulfate/polyacrylamide gels revelaed that, among 7 major proteins, band 1 and 2 proteins, both caoled spectrin, preferentially disappeared on the gels following X-irradiation (100-400 Gy [grays]). Spectrin was at least partially transformed into mutually cross-linked aggregates which did not enter the polyacrylamide gels. The most significant effect of the action of X-rays was the radiolytic fragmentation of spectrin to short polypeptide pieces having smaller molecular weights than the normal spectrin monomers. The effects of X-irradiation could also be detected with purified spectrin molecules. The other major protein bands, 3 to 7, did not diminish to a notable extent. X-rays induced changes in the shape of isolated ghosts with a dose-response relationship similar to that for the loss of bands 1 and 2 on the gels. Apparently the shape changes of ghosts might be the consequence of radiation-induced structural alterations of spectrin.

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