N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts
Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analys...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1973 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 330(1973), 3, Seite 356-361 |
| Übergeordnetes Werk: |
volume:330 ; year:1973 ; number:3 ; pages:356-361 |
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| 520 | |a Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. | ||
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(DE-627)NLEJ185725473 (DE-599)GBVNLZ185725473 DE-627 ger DE-627 rakwb eng N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Schmidt-Ullrich, R. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 330(1973), 3, Seite 356-361 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:330 year:1973 number:3 pages:356-361 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(73)90246-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 330 1973 3 356-361 |
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(DE-627)NLEJ185725473 (DE-599)GBVNLZ185725473 DE-627 ger DE-627 rakwb eng N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Schmidt-Ullrich, R. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 330(1973), 3, Seite 356-361 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:330 year:1973 number:3 pages:356-361 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(73)90246-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 330 1973 3 356-361 |
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(DE-627)NLEJ185725473 (DE-599)GBVNLZ185725473 DE-627 ger DE-627 rakwb eng N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Schmidt-Ullrich, R. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 330(1973), 3, Seite 356-361 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:330 year:1973 number:3 pages:356-361 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(73)90246-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 330 1973 3 356-361 |
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(DE-627)NLEJ185725473 (DE-599)GBVNLZ185725473 DE-627 ger DE-627 rakwb eng N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Schmidt-Ullrich, R. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 330(1973), 3, Seite 356-361 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:330 year:1973 number:3 pages:356-361 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(73)90246-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 330 1973 3 356-361 |
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(DE-627)NLEJ185725473 (DE-599)GBVNLZ185725473 DE-627 ger DE-627 rakwb eng N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Knufermann, H. oth Bhakdi, S. oth Schmidt-Ullrich, R. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 330(1973), 3, Seite 356-361 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:330 year:1973 number:3 pages:356-361 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(73)90246-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 330 1973 3 356-361 |
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n-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts |
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N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts |
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Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. |
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Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. |
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Preparative sodium dodecylsulfate-polyacrylamide gel electrophoresis of dansylated erythrocyte membrane proteins shows that 60% of the 1-dimethylaminophthalene-5-sulfonyl fluorescence migrates with sodium dodecylsulfate-polyacrylamide gel electrophoresis Bands 1,2 and 3. N-terminal amino acid analyses show that each of these bands contains at least five N-terminals. Bands 1 and 2 contain identical N-terminals. Most N-terminals appear constant, but sone additional N-termini vary from one donor to the next. |
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