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74 results on '"Luche, Sylvie"'

51. High Expression of Antioxidant Proteins in Dendritic Cells

Author

Rivollier, Aymeric, primary, Perrin-Cocon, Laure, additional, Luche, Sylvie, additional, Diemer, Hélène, additional, Strub, Jean-Marc, additional, Hanau, Daniel, additional, van Dorsselaer, Alain, additional, Lotteau, Vincent, additional, Rabourdin-Combe, Chantal, additional, Rabilloud, Thierry, additional, and Servet-Delprat, Christine, additional

Published
2006
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61. Detergents and Chaotropes for Protein Solubilization before Two-Dimensional Electrophoresis.

Author

Walker, John M., Thiellement, Hervé, Zivy, Michel, Damerval, Catherine, Méchin, Valérie, Rabilloud, Thierry, Luche, Sylvie, Santoni, Véronique, and Chevallet, Mireille

Abstract

Because of the outstanding separating capabilities of two-dimensional electrophoresis for complete proteins, it would be advantageous to be able to apply it to all types of proteins. Unfortunately, severe solubility problems hamper the analysis of many classes of proteins, but especially membrane proteins. These problems arise mainly in the extraction and isoelectric focusing steps, and solutions are sought to improve protein solubility under the conditions prevailing during isoelectric focusing. These solutions deal mainly with chaotropes and new detergents, which are both able to enhance protein solubility. The input of these compounds in proteomics analysis of membrane proteins is discussed, as well as future directions. [ABSTRACT FROM AUTHOR]

Published
2007
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62. Purification and Mass Spectrometry Identification of Microtubule-Binding Proteins From Xenopus Egg Extracts.

Author

Walker, John M., Jun Zhou, Gache, Vincent, Waridel, Patrice, Luche, Sylvie, Shevchenko, Andrej, and Popov, Andrei V.

Abstract

Microtubule-binding proteins are conveniently divided into two large groups: MAPs (microtubule-associated proteins), which can stabilize, anchor, and/or nucleate microtubules, and motors, which use the energy of ATP hydrolysis for a variety of functions, including microtubule network organization and cargo transportation along microtubules. Here, we describe the use of Taxol-stabilized microtubules for purification of MAPs, motors, and their complexes from Xenopus egg extracts. Isolated proteins are analysed using sodium dodecyl sulfate gel electrophoresis and identified by various mass spectrometry and database mining technologies. Found proteins can be grouped into three classes: (1) known MAPs and motors; (2) proteins previously reported as associated with the microtubule cytoskeleton, but without a clearly defined cytoskeletal function; (3) proteins not yet described as having microtubule localization. Sequence-similarity methods employed for protein identification allow efficient identification of MAPs and motors from species with yet unsequenced genomes. [ABSTRACT FROM AUTHOR]

Published
2007
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72. Purification and mass spectrometry identification of microtubule-binding proteins from Xenopus egg extracts.

Author

Gache V, Waridel P, Luche S, Shevchenko A, and Popov AV

Subjects
Animals, Brain ultrastructure, Cattle, Electrophoresis, Polyacrylamide Gel methods, Female, Paclitaxel chemistry, Tubulin chemistry, Xenopus laevis, Mass Spectrometry methods, Microtubule-Associated Proteins chemistry, Microtubule-Associated Proteins isolation & purification, Microtubules chemistry, Oocytes chemistry
Abstract

Microtubule-binding proteins are conveniently divided into two large groups: MAPs (microtubule-associated proteins), which can stabilize, anchor, and/or nucleate microtubules, and motors, which use the energy of ATP hydrolysis for a variety of functions, including microtubule network organization and cargo transportation along microtubules. Here, we describe the use of Taxol-stabilized microtubules for purification of MAPs, motors, and their complexes from Xenopus egg extracts. Isolated proteins are analysed using sodium dodecyl sulfate gel electrophoresis and identified by various mass spectrometry and database mining technologies. Found proteins can be grouped into three classes: (1) known MAPs and motors; (2) proteins previously reported as associated with the microtubule cytoskeleton, but without a clearly defined cytoskeletal function; (3) proteins not yet described as having microtubule localization. Sequence-similarity methods employed for protein identification allow efficient identification of MAPs and motors from species with yet unsequenced genomes.

Published
2007
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73. Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis.

Author

Rabilloud T, Luche S, Santoni V, and Chevallet M

Subjects
Arabidopsis chemistry, Isoelectric Focusing methods, Membrane Proteins chemistry, Plant Proteins chemistry, Proteomics instrumentation, Solubility, Solutions, Thiourea chemistry, Urea chemistry, Detergents chemistry, Electrophoresis, Gel, Two-Dimensional, Membrane Proteins isolation & purification, Plant Proteins isolation & purification, Proteomics methods
Abstract

Because of the outstanding separating capabilities of two-dimensional electrophoresis for complete proteins, it would be advantageous to be able to apply it to all types of proteins. Unfortunately, severe solubility problems hamper the analysis of many classes of proteins, but especially membrane proteins. These problems arise mainly in the extraction and isoelectric focusing steps, and solutions are sought to improve protein solubility under the conditions prevailing during isoelectric focusing. These solutions deal mainly with chaotropes and new detergents, which are both able to enhance protein solubility. The input of these compounds in proteomics analysis of membrane proteins is discussed, as well as future directions.

Published
2007
Full Text
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74. Preparing protein extracts for quantitative two-dimensional gel comparison.

Author

Chevallet M, Tastet C, Luche S, and Rabilloud T

Subjects
Animals, Buffers, Cell Nucleus chemistry, Humans, Organelles chemistry, Plant Proteins analysis, Electrophoresis, Gel, Two-Dimensional methods, Isoelectric Focusing methods, Proteins analysis, Tissue Extracts chemistry
Abstract

This unit describes basic protocols for efficient and reproducible protein solubilization from a variety of biological samples, including cultured animal cells and tissues, plant cells and tissues, bacteria, nuclei, other subcellular organelles, plasma, serum, and other biological fluids. The optimized extraction process is strongly sample-dependent and cannot be described for every type of sample. Instead, typical protocols are provided as general guidelines and illustrate good starting points for sample-preparation optimization. These solubilization procedures take into account the constraints brought by two-dimensional electrophoresis and are thus well suited for proteomic approaches.

Published
2004
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