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Your search keyword '"MESH : Detergents"' showing total 2 results
Start Over Descriptor "MESH : Detergents" Topic [ sdv.bbm.gtp ] life sciences [q-bio]/biochemistry, molecular biology/genomics [q-bio.gn]
2 results on '"MESH : Detergents"'

1. Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis

Author

Rabilloud, Thierry, Biochimie et biophysique des systèmes intégrés (BBSI), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Biochimie et biophysique des systèmes intégrés ( BBSI ), and Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
Erythrocytes, MESH : Isoelectric Focusing, Detergents, Chemical Fractionation, MESH: Thiourea, MESH: Chemical Fractionation, MESH : Urea, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Humans, Urea, Quantitative Biology - Genomics, MESH : Thiourea, Electrophoresis, Gel, Two-Dimensional, MESH: Urea, Genomics (q-bio.GN), MESH: Hydrophobicity, MESH: Humans, MESH : Chemical Fractionation, MESH : Solubility, MESH: Erythrocytes, MESH : Humans, Thiourea, Membrane Proteins, MESH : Detergents, MESH : Electrophoresis, Gel, Two-Dimensional, MESH: Electrophoresis, Gel, Two-Dimensional, MESH: Solubility, Solubility, MESH : Membrane Proteins, [ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], FOS: Biological sciences, MESH: Isoelectric Focusing, MESH : Hydrophobicity, MESH: Membrane Proteins, Isoelectric Focusing, Hydrophobic and Hydrophilic Interactions, MESH : Erythrocytes, MESH: Detergents
Abstract

International audience; Because of the outstanding ability of two-dimensional electrophoresis to separate complex mixtures of intact proteins, it would be advantageous to apply it to all types of proteins, including hydrophobic and membrane proteins. Unfortunately, poor solubility hampers the analysis of these molecules. As these problems arise mainly in the extraction and isoelectric focusing steps, the solution is to improve protein solubility under the conditions prevailing during isoelectric focusing. This chapter describes the use of chaotropes and novel detergents to enhance protein solubility during sample extraction and isoelectric focussing, and discusses the contribution of these compounds to improving proteomic analysis of membrane proteins.

Published
2009

2. The stress proteome of Enterococcus faecalis

Author

J C, Giard, J M, Laplace, A, Rincé, V, Pichereau, A, Benachour, C, Leboeuf, S, Flahaut, Y, Auffray, A, Hartke, Laboratoire de Microbiologie de l’Environnement (LME), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Recherche Agronomique (INRA), Laboratoire des Sciences de l'Environnement Marin (LEMAR) (LEMAR), Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU), Institut de Recherche pour le Développement (IRD)-Institut Universitaire Européen de la Mer (IUEM), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Microbiologie de l’Environnement ( LME ), Institut National de la Recherche Agronomique ( INRA ) -Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ), Laboratoire des Sciences de l'Environnement Marin (LEMAR) ( LEMAR ), Institut de Recherche pour le Développement ( IRD ) -Institut Français de Recherche pour l'Exploitation de la Mer ( IFREMER ) -Université de Brest ( UBO ) -Institut Universitaire Européen de la Mer ( IUEM ), Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD ) -Université de Brest ( UBO ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD ) -Université de Brest ( UBO ) -Centre National de la Recherche Scientifique ( CNRS ), and Institut de Recherche pour le Développement (IRD)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH : Oxidative Stress, MESH : Molecular Sequence Data, Proteome, MESH: Sequence Homology, Amino Acid, MESH : Enzymes, Sequence Homology, MESH : Blotting, Western, MESH: Amino Acid Sequence, [ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH : Mercuric Chloride, MESH: Silver Staining, Cadmium Chloride, Enterococcus faecalis, MESH : Bacterial Proteins, MESH : Silver Staining, Electrophoresis, Gel, Two-Dimensional, MESH : Enterococcus faecalis, Databases, Protein, MESH: Bacterial Proteins, MESH: Cadmium Chloride, Gel, MESH: Gene Expression Regulation, Bacterial, MESH: Oxidative Stress, Blotting, MESH : Amino Acid Sequence, Bacterial, Sodium Dodecyl Sulfate, MESH : Sequence Homology, Amino Acid, Enzymes, DNA-Binding Proteins, MESH: Glucose, MESH: Proteome, Amino Acid, [ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], MESH: Repressor Proteins, Two-Dimensional, Mercuric Chloride, MESH: Hydrogen Peroxide, MESH : DNA-Binding Proteins, MESH : Repressor Proteins, Western, MESH : Gene Expression Regulation, Bacterial, Electrophoresis, MESH: Sodium Dodecyl Sulfate, MESH: Databases, Protein, Silver Staining, MESH: Enterococcus faecalis, MESH: Terminology as Topic, MESH : Cadmium Chloride, Blotting, Western, Detergents, Molecular Sequence Data, MESH : Acids, MESH: Enzymes, MESH : Proteome, MESH : Open Reading Frames, MESH: Bile Acids and Salts, MESH: Acids, Bile Acids and Salts, Databases, Open Reading Frames, Bacterial Proteins, Terminology as Topic, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], MESH: Blotting, Western, Amino Acid Sequence, MESH : Databases, Protein, MESH: Mercuric Chloride, MESH : Sodium Dodecyl Sulfate, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, MESH : Glucose, Protein, Gene Expression Regulation, Bacterial, MESH : Detergents, MESH : Electrophoresis, Gel, Two-Dimensional, Hydrogen Peroxide, MESH: Open Reading Frames, MESH: Electrophoresis, Gel, Two-Dimensional, MESH : Terminology as Topic, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH : Bile Acids and Salts, Repressor Proteins, Oxidative Stress, Glucose, Gene Expression Regulation, MESH : Hydrogen Peroxide, Acids, MESH: DNA-Binding Proteins, MESH: Detergents
Abstract

International audience; Enterococcus faecalis is a resident bacterium of the intestinal tract of humans and animals. This bacterium can be responsible for serious diseases and is one of the largest causes of hospital-based infections. This hardy organism resists many kinds of stresses and is used as a major indicator of the hygienic quality of food, milk, and drinking water. On the other side, enterococci seem to have beneficial role in the development of cheese aroma and are added in certain starter cultures. Since ten years, our laboratory has used the two-dimensional electrophoresis (2-DE) technique to study the response of E. faecalis to physical or chemical stresses as well as to glucose and total starvation. Twenty-seven protein spots on 2-D gels have been identified by N-terminal sequencing or Western blotting which make up the first proteome database of this species. The proteins were classified in four different groups according to their function and their regulation. The first group comprises well-characterized proteins with known protective functions towards stresses. The second group contains enzymes of catabolic pathways. Their implication in stress resistance seems not obvious. A third group are proteins induced in glucose-starved cells belonging to the CcpA regulon. Induction of these enzymes under starvation may serve to increase the scavenging capacity of the cells for nutrients or may be important to mobilize endogenous energetic reserves. Lastly, nine N-terminal amino acid sequences or open reading frames (ORF) showed no homologies with sequences in databases. A comprehensive description of stress proteins of E. faecalis and analysis of their patterns of expression under different environmental conditions would greatly increase our understanding of the molecular mechanisms underlying the extraordinary capacity of this bacterium to survive under hostile conditions.

Published
2001

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