Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate
1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine...
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 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 389(1975), 3, Seite 464-476 |
| Übergeordnetes Werk: |
volume:389 ; year:1975 ; number:3 ; pages:464-476 |
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| 245 | 1 | 0 | |a Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate |
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| 520 | |a 1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. | ||
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(DE-627)NLEJ185721265 (DE-599)GBVNLZ185721265 DE-627 ger DE-627 rakwb eng Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 389(1975), 3, Seite 464-476 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:389 year:1975 number:3 pages:464-476 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90157-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 389 1975 3 464-476 |
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(DE-627)NLEJ185721265 (DE-599)GBVNLZ185721265 DE-627 ger DE-627 rakwb eng Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 389(1975), 3, Seite 464-476 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:389 year:1975 number:3 pages:464-476 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90157-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 389 1975 3 464-476 |
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(DE-627)NLEJ185721265 (DE-599)GBVNLZ185721265 DE-627 ger DE-627 rakwb eng Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 389(1975), 3, Seite 464-476 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:389 year:1975 number:3 pages:464-476 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90157-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 389 1975 3 464-476 |
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(DE-627)NLEJ185721265 (DE-599)GBVNLZ185721265 DE-627 ger DE-627 rakwb eng Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 389(1975), 3, Seite 464-476 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:389 year:1975 number:3 pages:464-476 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90157-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 389 1975 3 464-476 |
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(DE-627)NLEJ185721265 (DE-599)GBVNLZ185721265 DE-627 ger DE-627 rakwb eng Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate 1975 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 389(1975), 3, Seite 464-476 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:389 year:1975 number:3 pages:464-476 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90157-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 389 1975 3 464-476 |
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We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. 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rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate |
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Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate |
| abstract |
1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. |
| abstractGer |
1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. |
| abstract_unstemmed |
1. We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. Some additional N-terminal amino acids vary from one donor to the next. |
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Rapid preparative isolation of major erythrocyte membrane proteins using polyacrylamide gel electrophoresis in sodium dodecylsulfate |
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Knufermann, H. Bhakdi, S. Wallach, D.F.H. |
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We describe a simple method for preparative, sodium dodecylsulfate/polyacrylamide gel electrophoresis of the major proteins in human erythrocyte membranes.2. The method is based on extraction of prestained proteins from gel slabs. Three different fluorescent dyes (o-phthalaldehyde, fluorescamine and 1-dimethylaminonaphthalene-5-sulfonylchloride) have been used for prestaining. The method allows separation of up to 75 mg membrane protein and isolation of mg quantities of all major erythrocyte ghost proteins, while preserving the high resolution of analytical polyacrylamide gel electrophoresis.3. Yield depends on extraction conditions and the molecular weight of the proteins being eluted. It ranges from 43-48 % for protein 1 (apparent mol. wt approx. 310 000) and 72-78 % for protein 3 (apparent mol. wt 87 000-93 000) to 87-93 % for protein 6 (apparent mol. wt 35 000).4. The labile behaviour of the high molecular ''spectrin'' bands (bands 1 and 2) is described. Extraction at room temperature tends to split these proteins into products of lower molecular weight. In contrast, the minor protein components 2.1 and 2.2 tend to aggregate yielding components 1 and 2.5. N-terminal amino acid analyses have been performed on proteins 1, 2, 3, 4A, 4B, 5 and 6. Each of these bands contains several N-terminals, most of which appear constant. 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7.40026 |