Effect of in vivo γ-irradiation on the binding of wheat germ agglutinin on lymphocyte plasma membranes
Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper de...
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Published in | Biochimica et biophysica acta Vol. 883; no. 3; pp. 407 - 412 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
01.10.1986
Elsevier North-Holland |
Subjects | |
Online Access | Get full text |
ISSN | 0304-4165 0006-3002 1872-8006 |
DOI | 10.1016/0304-4165(86)90277-1 |
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Abstract | Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper demonstrates that below an irradiation level of 1 gray (Gy), removal of sialic acid is the major feature leading to new exposed specific binding sites for wheat germ agglutinin, since this lectin is specific for sialic acid and
N-
acetyl-
D-glucosamine
. Our studies also suggest that above 1 Gy of irradiation more internal damage occurs, since we observed a striking decrease in wheat germ agglutinin binding sites. |
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AbstractList | Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper demonstrates that below an irradiation level of 1 gray (Gy), removal of sialic acid is the major feature leading to new exposed specific binding sites for wheat germ agglutinin, since this lectin is specific for sialic acid and N-acetyl-D-glucosamine. Our studies also suggest that above 1 Gy of irradiation more internal damage occurs, since we observed a striking decrease in wheat germ agglutinin binding sites.Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper demonstrates that below an irradiation level of 1 gray (Gy), removal of sialic acid is the major feature leading to new exposed specific binding sites for wheat germ agglutinin, since this lectin is specific for sialic acid and N-acetyl-D-glucosamine. Our studies also suggest that above 1 Gy of irradiation more internal damage occurs, since we observed a striking decrease in wheat germ agglutinin binding sites. Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper demonstrates that below an irradiation level of 1 gray (Gy), removal of sialic acid is the major feature leading to new exposed specific binding sites for wheat germ agglutinin, since this lectin is specific for sialic acid and N- acetyl- D-glucosamine . Our studies also suggest that above 1 Gy of irradiation more internal damage occurs, since we observed a striking decrease in wheat germ agglutinin binding sites. Using quantitative fluorimetry with fluoresceinated wheat germ agglutinin, we have been able to investigate in vivo gamma radiation-induced damage at the outer membrane level of rat splenic lymphocytes, namely damage to the glucosidic moieties of membrane glycoproteins and glycolipids. This paper demonstrates that below an irradiation level of 1 gray (Gy), removal of sialic acid is the major feature leading to new exposed specific binding sites for wheat germ agglutinin, since this lectin is specific for sialic acid and N-acetyl-D-glucosamine. Our studies also suggest that above 1 Gy of irradiation more internal damage occurs, since we observed a striking decrease in wheat germ agglutinin binding sites. |
Author | Daveloose, Denis Leterrier, Francois Hoebeke, Johan Moullier, Philippe Dubos, Michel |
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Cites_doi | 10.1016/0014-4827(77)90161-6 10.1111/j.1432-1033.1979.tb13040.x 10.1016/0008-8749(76)90162-3 10.1016/0014-4827(76)90640-6 10.1016/0003-2697(67)90297-7 10.1016/0014-4827(75)90155-X 10.1021/bi00616a022 10.1080/09553008114551061 10.1016/0006-291X(82)90666-0 10.1007/BF01407598 10.1016/0161-5890(80)90123-6 10.1080/09553008114551051 10.1111/j.1432-1033.1979.tb13157.x 10.1002/eji.1830040309 10.1111/j.1432-1033.1980.tb04410.x 10.1038/259507a0 10.2307/3574444 |
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Keywords | Lectin Ionizing radiation Mitogen receptor Rat lymphocyte Cell culture Flow cytometry Rat Rodentia Wheat germ Molecular interaction Fluorescence spectrometry Vertebrata Gamma irradiation Mammalia Animal Agglutinin Plasma membrane Mitogen Lymphocyte |
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SubjectTerms | Animals Biological and medical sciences Biological effects of radiation Cell Membrane - metabolism Cell Membrane - radiation effects Fundamental and applied biological sciences. Psychology Gamma Rays Ionizing radiation Ionizing radiations Lectin Lymphocytes - metabolism Lymphocytes - radiation effects Male Mitogen receptor Rat lymphocyte Rats Rats, Inbred Strains Receptors, Mitogen - radiation effects Tissues, organs and organisms biophysics Wheat Germ Agglutinins - metabolism |
Title | Effect of in vivo γ-irradiation on the binding of wheat germ agglutinin on lymphocyte plasma membranes |
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