Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system
Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a pro...
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1983 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Journal of Chromatography A - Amsterdam : Elsevier, 260(1983), Seite 329-336 |
| Übergeordnetes Werk: |
volume:260 ; year:1983 ; pages:329-336 |
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NLEJ174175817 |
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| 520 | |a Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. | ||
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(DE-627)NLEJ174175817 (DE-599)GBVNLZ174175817 DE-627 ger DE-627 rakwb eng Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zaslavsky, B.Y. oth Mestechkina, N.M. oth Rogozhin, S.V. oth in Journal of Chromatography A Amsterdam : Elsevier 260(1983), Seite 329-336 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:260 year:1983 pages:329-336 http://linkinghub.elsevier.com/retrieve/pii/0021-9673(83)80040-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 260 1983 329-336 |
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(DE-627)NLEJ174175817 (DE-599)GBVNLZ174175817 DE-627 ger DE-627 rakwb eng Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zaslavsky, B.Y. oth Mestechkina, N.M. oth Rogozhin, S.V. oth in Journal of Chromatography A Amsterdam : Elsevier 260(1983), Seite 329-336 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:260 year:1983 pages:329-336 http://linkinghub.elsevier.com/retrieve/pii/0021-9673(83)80040-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 260 1983 329-336 |
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(DE-627)NLEJ174175817 (DE-599)GBVNLZ174175817 DE-627 ger DE-627 rakwb eng Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zaslavsky, B.Y. oth Mestechkina, N.M. oth Rogozhin, S.V. oth in Journal of Chromatography A Amsterdam : Elsevier 260(1983), Seite 329-336 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:260 year:1983 pages:329-336 http://linkinghub.elsevier.com/retrieve/pii/0021-9673(83)80040-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 260 1983 329-336 |
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(DE-627)NLEJ174175817 (DE-599)GBVNLZ174175817 DE-627 ger DE-627 rakwb eng Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zaslavsky, B.Y. oth Mestechkina, N.M. oth Rogozhin, S.V. oth in Journal of Chromatography A Amsterdam : Elsevier 260(1983), Seite 329-336 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:260 year:1983 pages:329-336 http://linkinghub.elsevier.com/retrieve/pii/0021-9673(83)80040-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 260 1983 329-336 |
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(DE-627)NLEJ174175817 (DE-599)GBVNLZ174175817 DE-627 ger DE-627 rakwb eng Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Zaslavsky, B.Y. oth Mestechkina, N.M. oth Rogozhin, S.V. oth in Journal of Chromatography A Amsterdam : Elsevier 260(1983), Seite 329-336 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:260 year:1983 pages:329-336 http://linkinghub.elsevier.com/retrieve/pii/0021-9673(83)80040-5 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 260 1983 329-336 |
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characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system |
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Characteristics of protein-aqueous medium interactions measured by partition in aqueous ficoll-dextran biphasic system |
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Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. |
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Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. |
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Partitioning of a number of proteins in the aqueous Ficoll-400-Dextran-70 biphasic system was studied at pH 7.4 under varied ionic compositions. The relative hydrophobicities of the proteins have been estimated, and the contributions of the interactions of the ionogenic and non-ionic groups of a protein with an aqueous environment to the total hydrophobicity of the protein have been evaluated. Some arguments in support of the biological significance of the effect of ionic composition on the relative hydrophobicity of biological macromolecules are given. Possible applications of the partition technique to protein research are discussed. |
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