Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry
The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1981 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 640(1981), 2, Seite 535-543 |
| Übergeordnetes Werk: |
volume:640 ; year:1981 ; number:2 ; pages:535-543 |
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NLEJ185847374 |
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| 245 | 1 | 0 | |a Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry |
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| 520 | |a The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. | ||
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(DE-627)NLEJ185847374 (DE-599)GBVNLZ185847374 DE-627 ger DE-627 rakwb eng Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Haest, C.W.M. oth Kamp, D. oth Deuticke, B. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 640(1981), 2, Seite 535-543 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:640 year:1981 number:2 pages:535-543 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90477-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 640 1981 2 535-543 |
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(DE-627)NLEJ185847374 (DE-599)GBVNLZ185847374 DE-627 ger DE-627 rakwb eng Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Haest, C.W.M. oth Kamp, D. oth Deuticke, B. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 640(1981), 2, Seite 535-543 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:640 year:1981 number:2 pages:535-543 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90477-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 640 1981 2 535-543 |
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(DE-627)NLEJ185847374 (DE-599)GBVNLZ185847374 DE-627 ger DE-627 rakwb eng Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Haest, C.W.M. oth Kamp, D. oth Deuticke, B. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 640(1981), 2, Seite 535-543 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:640 year:1981 number:2 pages:535-543 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90477-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 640 1981 2 535-543 |
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(DE-627)NLEJ185847374 (DE-599)GBVNLZ185847374 DE-627 ger DE-627 rakwb eng Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Haest, C.W.M. oth Kamp, D. oth Deuticke, B. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 640(1981), 2, Seite 535-543 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:640 year:1981 number:2 pages:535-543 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90477-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 640 1981 2 535-543 |
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(DE-627)NLEJ185847374 (DE-599)GBVNLZ185847374 DE-627 ger DE-627 rakwb eng Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Haest, C.W.M. oth Kamp, D. oth Deuticke, B. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 640(1981), 2, Seite 535-543 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:640 year:1981 number:2 pages:535-543 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90477-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 640 1981 2 535-543 |
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Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry |
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The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. |
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The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. |
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The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ185847374</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707030403.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1981 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185847374</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185847374</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Penetration of 2,4,6-trinitrobenzenesulfonate into human erythrocytes - Consequences for studies on phospholipid asymmetry</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1981</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The glutathione content of human erythrocytes rapidly diminishes when cells are exposed to 2,4,6-trinitrobenzenesulfonate (20 μmol/l cells) at 37^oC. Even at 0^oC a slow decrease in glutathione content is observed. The uptake of trinitrobenzenesulfonate by the cells is retarded by inhibitors of the inorganic anion exchange system, indicating that trinitrobenzenesulfonate enters the cells by this pathway.The disappearance of glutathione most probably results from the reaction: 2 GSH + trinitrobenzenesulfonate -> GSSG + aminodinitrobenzenesulfonate The reaction of trinitrobenzenesulfonate with glutathione occurs prior to its covalent binding to amino groups of hemoglobin which makes this reaction a more sensitive method of detection of penetration of trinitrobenzenesulfonate into erythrocytes. Results of studies on the asymmetric distribution of phospholipids using trinitrobenzenesulfonate as the only probe should be reconsidered in the light of these new data.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Haest, C.W.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kamp, D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Deuticke, B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Biomembranes</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">640(1981), 2, Seite 535-543</subfield><subfield code="w">(DE-627)NLEJ185706983</subfield><subfield code="w">(DE-600)2209384-9</subfield><subfield code="x">0005-2736</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:640</subfield><subfield code="g">year:1981</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:535-543</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90477-6</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">640</subfield><subfield code="j">1981</subfield><subfield code="e">2</subfield><subfield code="h">535-543</subfield></datafield></record></collection>
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