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Analytical Biochemistry
Hempel, K., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Rosen, R., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany, Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Becher, D., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Büttner, K., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Hecker, M., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Ron, E.Z., Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Ultra acidic proteins, generated by posttranslational modifications, are becoming increasingly important due to recent evidence showing their function as regulatory elements or as intermediates in degradation pathways in bacteria. Such proteins are important in neurodegenerative diseases and embryonic development, and they include the Alzheimer-related tau (τ) protein (resulting from posttranslational modifications) and the phosphor-storage embryonic proteins. The ultra acidic proteins are difficult to study because standard two-dimensional gel electrophoresis is inadequate for their analysis. Here we describe a novel electrophoresis system of anodic acidic gels that can replace isoelectric focusing as the first dimension of separation in two-dimensional electrophoresis. The system is based on a sodium acetate buffer (pH 4.6), is compatible with traditional stains (e.g., Coomassie blue) as well as novel fluorescent dyes (e.g., Pro-Q Diamond), and is quantitative for the analysis of ultra acidic proteins. The anodic acidic gels were used for the functional classification of the ultra acidic part of the Bacillus subtilis proteome, showing significant improvement over traditional two-dimensional electrophoresis. © 2008 Elsevier Inc. All rights reserved.
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תנאי שימוש
Analysis of ultra acidic proteins by the use of anodic acidic gels
385
Hempel, K., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Rosen, R., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany, Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Becher, D., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Büttner, K., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Hecker, M., Institut für Mikrobiologie, Ernst Moritz Arndt Universität Greifswald, D-17487 Greifswald, Germany
Ron, E.Z., Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel Aviv, Israel
Analysis of ultra acidic proteins by the use of anodic acidic gels
Ultra acidic proteins, generated by posttranslational modifications, are becoming increasingly important due to recent evidence showing their function as regulatory elements or as intermediates in degradation pathways in bacteria. Such proteins are important in neurodegenerative diseases and embryonic development, and they include the Alzheimer-related tau (τ) protein (resulting from posttranslational modifications) and the phosphor-storage embryonic proteins. The ultra acidic proteins are difficult to study because standard two-dimensional gel electrophoresis is inadequate for their analysis. Here we describe a novel electrophoresis system of anodic acidic gels that can replace isoelectric focusing as the first dimension of separation in two-dimensional electrophoresis. The system is based on a sodium acetate buffer (pH 4.6), is compatible with traditional stains (e.g., Coomassie blue) as well as novel fluorescent dyes (e.g., Pro-Q Diamond), and is quantitative for the analysis of ultra acidic proteins. The anodic acidic gels were used for the functional classification of the ultra acidic part of the Bacillus subtilis proteome, showing significant improvement over traditional two-dimensional electrophoresis. © 2008 Elsevier Inc. All rights reserved.
Scientific Publication
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