Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate
1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1974 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 345(1974), 3, Seite 448-457 |
| Übergeordnetes Werk: |
volume:345 ; year:1974 ; number:3 ; pages:448-457 |
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NLEJ185729630 |
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| 245 | 1 | 0 | |a Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate |
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| 520 | |a 1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. | ||
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(DE-627)NLEJ185729630 (DE-599)GBVNLZ185729630 DE-627 ger DE-627 rakwb eng Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 345(1974), 3, Seite 448-457 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:345 year:1974 number:3 pages:448-457 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90205-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 345 1974 3 448-457 |
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(DE-627)NLEJ185729630 (DE-599)GBVNLZ185729630 DE-627 ger DE-627 rakwb eng Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 345(1974), 3, Seite 448-457 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:345 year:1974 number:3 pages:448-457 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90205-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 345 1974 3 448-457 |
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(DE-627)NLEJ185729630 (DE-599)GBVNLZ185729630 DE-627 ger DE-627 rakwb eng Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 345(1974), 3, Seite 448-457 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:345 year:1974 number:3 pages:448-457 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90205-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 345 1974 3 448-457 |
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(DE-627)NLEJ185729630 (DE-599)GBVNLZ185729630 DE-627 ger DE-627 rakwb eng Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 345(1974), 3, Seite 448-457 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:345 year:1974 number:3 pages:448-457 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90205-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 345 1974 3 448-457 |
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(DE-627)NLEJ185729630 (DE-599)GBVNLZ185729630 DE-627 ger DE-627 rakwb eng Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 345(1974), 3, Seite 448-457 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:345 year:1974 number:3 pages:448-457 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90205-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 345 1974 3 448-457 |
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Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate |
| abstract |
1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. |
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1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. |
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1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins. |
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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">NLEJ185729630</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707024408.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1974 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185729630</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185729630</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">Separation of EDTA-extractable erythrocyte membrane proteins by isoelectric focussing linked to electrophoresis in sodium dodecyl sulfate</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1974</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">1. EDTA-extractable proteins of human erythrocyte membranes can be separated in 8 M urea by isoelectric focussing in polyacrylamide gels2. Subsequent electrophoresis at right angles in sodium dodecyl sulfate-laden polyacrylamide shows that most of the bands hitherto defined by simple sodium dodecyl sulfate polyacrylamide gel electrophoresis do not represent single proteins/peptides, but comprise mixtures of diverse molecular species with different isoelectric points.3. The high molecular weight sodium dodecyl sulfate bands 1,2,2.1 and 2.2 possess identical isoelectric points. The isoelectric points and Band 5 components also overlap with those of the Bands 1, 2, 2.1 and 2.2. This suggests a structural relationship between these entities.4. Membranes from different donors show slight variations in the two-dimensional electrophoretic pattern.5. The separation techniques presented here provide greater resolution than hitherto attained and should prove useful for the detailed analysis and characterisation of membrane proteins.</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">Bhakdi, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Knufermann, H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wallach, D.F.H.</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">345(1974), 3, Seite 448-457</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:345</subfield><subfield code="g">year:1974</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:448-457</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90205-3</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">345</subfield><subfield code="j">1974</subfield><subfield code="e">3</subfield><subfield code="h">448-457</subfield></datafield></record></collection>
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