Two-dimensional separation of erythrocyte membrane proteins
1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1975 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 394(1975), 4, Seite 550-557 |
| Übergeordnetes Werk: |
volume:394 ; year:1975 ; number:4 ; pages:550-557 |
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NLEJ185716741 |
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| 245 | 1 | 0 | |a Two-dimensional separation of erythrocyte membrane proteins |
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| 520 | |a 1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. | ||
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(DE-627)NLEJ185716741 (DE-599)GBVNLZ185716741 DE-627 ger DE-627 rakwb eng Two-dimensional separation of erythrocyte membrane proteins 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. 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 394(1975), 4, Seite 550-557 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:394 year:1975 number:4 pages:550-557 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90140-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 394 1975 4 550-557 |
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(DE-627)NLEJ185716741 (DE-599)GBVNLZ185716741 DE-627 ger DE-627 rakwb eng Two-dimensional separation of erythrocyte membrane proteins 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. 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 394(1975), 4, Seite 550-557 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:394 year:1975 number:4 pages:550-557 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90140-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 394 1975 4 550-557 |
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(DE-627)NLEJ185716741 (DE-599)GBVNLZ185716741 DE-627 ger DE-627 rakwb eng Two-dimensional separation of erythrocyte membrane proteins 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. 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 394(1975), 4, Seite 550-557 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:394 year:1975 number:4 pages:550-557 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90140-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 394 1975 4 550-557 |
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(DE-627)NLEJ185716741 (DE-599)GBVNLZ185716741 DE-627 ger DE-627 rakwb eng Two-dimensional separation of erythrocyte membrane proteins 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. 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 394(1975), 4, Seite 550-557 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:394 year:1975 number:4 pages:550-557 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90140-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 394 1975 4 550-557 |
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(DE-627)NLEJ185716741 (DE-599)GBVNLZ185716741 DE-627 ger DE-627 rakwb eng Two-dimensional separation of erythrocyte membrane proteins 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. 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 394(1975), 4, Seite 550-557 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:394 year:1975 number:4 pages:550-557 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90140-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 394 1975 4 550-557 |
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Two-dimensional separation of erythrocyte membrane proteins |
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1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. |
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1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. |
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1). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure. |
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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">NLEJ185716741</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707024202.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1975 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185716741</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185716741</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">Two-dimensional separation of erythrocyte membrane proteins</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1975</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). Erythrocyte membrane proteins eluted with Triton X-100 or dilute EDTA have been separated two-dimensionally by isoelectric focusing in polyacrylamide gels containing 1% Triton X-100 plus 8 M urea, followed by electrophoresis using sodium dodecyl sulfate. Characteristic patterns, consistent among 40 healthy donors, were obtained.2. The resulting patterns contain at least 30 components. The ''spectrin'' components (sodium dodecyl sulfate Bands 1 and 2) focus in the same pH range. Other membrane components giving single bands in sodium dodecyl sulfate electrophoresis appear to be heterogeneous.3. Triton X-100, but not EDTA, extracts the principal membrane glycoproteins and major ''intrinsic'' protein. Otherwise, proteins preferentially eluted by EDTA extract poorly with Triton X-100 and vice versa.4. Membrane glycoproteins migrate anodally during electrofocusing and can be purified in a simple, one-step procedure.</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">394(1975), 4, Seite 550-557</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:394</subfield><subfield code="g">year:1975</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:550-557</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90140-6</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">394</subfield><subfield code="j">1975</subfield><subfield code="e">4</subfield><subfield code="h">550-557</subfield></datafield></record></collection>
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