Radiation-Induced Structural Changes in Human Erythrocyte Membrane Proteins Revealed by Sodium Dodecyl Sulfate/Polyacrylamide Gel Electrophoresis
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 revealed that, among seven major proteins, band 1 and 2 proteins, both called...
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description | 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 revealed that, among seven major proteins, band 1 and 2 proteins, both called spectrin, preferentially disappeared on the gels following X irradiation (100-400 Gy). Spectrin was at least partly 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. These 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. It was also observed that X rays induce 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. It is suggested that the shape changes of ghosts might be the consequence of radiation-induced structural alterations of spectrin. |
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The electrophoretic patterns on sodium dodecyl sulfate/polyacrylamide gels revealed that, among seven major proteins, band 1 and 2 proteins, both called spectrin, preferentially disappeared on the gels following X irradiation (100-400 Gy). Spectrin was at least partly 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. These 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. It was also observed that X rays induce 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. It is suggested that the shape changes of ghosts might be the consequence of radiation-induced structural alterations of spectrin.</description><identifier>ISSN: 0033-7587</identifier><identifier>EISSN: 1938-5404</identifier><identifier>DOI: 10.2307/3575785</identifier><identifier>PMID: 7063622</identifier><language>eng</language><publisher>United States: Academic Press, Inc</publisher><subject>560122 - Radiation Effects on Cells- Internal Source- (-1987) ; BIOLOGICAL EFFECTS ; BIOLOGICAL MATERIALS ; BIOLOGICAL RADIATION EFFECTS ; BLOOD ; BLOOD CELLS ; BODY FLUIDS ; Dose-Response Relationship, Radiation ; ELECTROMAGNETIC RADIATION ; Electrophoresis ; Electrophoresis, Polyacrylamide Gel ; Erythrocyte membrane ; Erythrocyte Membrane - radiation effects ; ERYTHROCYTES ; Erythrocytes - radiation effects ; Gels ; Humans ; INDUCTION ; IONIZING RADIATIONS ; Irradiation ; man ; MATERIALS ; Membrane proteins ; Membrane Proteins - radiation effects ; Molecular spectra ; ORGANIC COMPOUNDS ; PROTEINS ; Radiation dosage ; RADIATION EFFECTS ; RADIATION, THERMAL, AND OTHER ENVIRON. 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Res.; (United States)</title><addtitle>Radiat Res</addtitle><description>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 revealed that, among seven major proteins, band 1 and 2 proteins, both called spectrin, preferentially disappeared on the gels following X irradiation (100-400 Gy). Spectrin was at least partly 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. These 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. It was also observed that X rays induce 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. It is suggested that the shape changes of ghosts might be the consequence of radiation-induced structural alterations of spectrin.</description><subject>560122 - Radiation Effects on Cells- Internal Source- (-1987)</subject><subject>BIOLOGICAL EFFECTS</subject><subject>BIOLOGICAL MATERIALS</subject><subject>BIOLOGICAL RADIATION EFFECTS</subject><subject>BLOOD</subject><subject>BLOOD CELLS</subject><subject>BODY FLUIDS</subject><subject>Dose-Response Relationship, Radiation</subject><subject>ELECTROMAGNETIC RADIATION</subject><subject>Electrophoresis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Erythrocyte membrane</subject><subject>Erythrocyte Membrane - radiation effects</subject><subject>ERYTHROCYTES</subject><subject>Erythrocytes - radiation effects</subject><subject>Gels</subject><subject>Humans</subject><subject>INDUCTION</subject><subject>IONIZING RADIATIONS</subject><subject>Irradiation</subject><subject>man</subject><subject>MATERIALS</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - radiation effects</subject><subject>Molecular spectra</subject><subject>ORGANIC COMPOUNDS</subject><subject>PROTEINS</subject><subject>Radiation dosage</subject><subject>RADIATION EFFECTS</subject><subject>RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. 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Res.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Todo, Takeshi</au><au>Yonei, Shuji</au><au>Kato, Mikita</au><aucorp>Kyoto Univ., Japan</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Radiation-Induced Structural Changes in Human Erythrocyte Membrane Proteins Revealed by Sodium Dodecyl Sulfate/Polyacrylamide Gel Electrophoresis</atitle><jtitle>Radiat. Res.; (United States)</jtitle><addtitle>Radiat Res</addtitle><date>1982-02</date><risdate>1982</risdate><volume>89</volume><issue>2</issue><spage>408</spage><epage>419</epage><pages>408-419</pages><issn>0033-7587</issn><eissn>1938-5404</eissn><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 revealed that, among seven major proteins, band 1 and 2 proteins, both called spectrin, preferentially disappeared on the gels following X irradiation (100-400 Gy). Spectrin was at least partly 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. These 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. It was also observed that X rays induce 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. It is suggested that the shape changes of ghosts might be the consequence of radiation-induced structural alterations of spectrin.</abstract><cop>United States</cop><pub>Academic Press, Inc</pub><pmid>7063622</pmid><doi>10.2307/3575785</doi><tpages>12</tpages></addata></record> |
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subjects | 560122 - Radiation Effects on Cells- Internal Source- (-1987) BIOLOGICAL EFFECTS BIOLOGICAL MATERIALS BIOLOGICAL RADIATION EFFECTS BLOOD BLOOD CELLS BODY FLUIDS Dose-Response Relationship, Radiation ELECTROMAGNETIC RADIATION Electrophoresis Electrophoresis, Polyacrylamide Gel Erythrocyte membrane Erythrocyte Membrane - radiation effects ERYTHROCYTES Erythrocytes - radiation effects Gels Humans INDUCTION IONIZING RADIATIONS Irradiation man MATERIALS Membrane proteins Membrane Proteins - radiation effects Molecular spectra ORGANIC COMPOUNDS PROTEINS Radiation dosage RADIATION EFFECTS RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT RADIATIONS RADIOSENSITIVITY Sodium Dodecyl Sulfate Solar X rays Spectrin - radiation effects X RADIATION X ray spectrum |
title | Radiation-Induced Structural Changes in Human Erythrocyte Membrane Proteins Revealed by Sodium Dodecyl Sulfate/Polyacrylamide Gel Electrophoresis |
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