Patrick Rouimi | Université de Toulouse III Paul Sabatier (original) (raw)
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Papers by Patrick Rouimi
HAL (Le Centre pour la Communication Scientifique Directe), 1995
A method is described to study the precise positioning of transmembrane peptides in a phospholipi... more A method is described to study the precise positioning of transmembrane peptides in a phospholipid bilayer combining hydrogen/deuterium (H/D) exchange and nanoelectrospray ionization mass spectrometry. The method was tested by using model systems consisting of designed α-helical transmembrane peptides [acetylGW 2 (LA) 5 W 2 Aethanolamine (WALP16) and acetyl-(GA) 3 W 2 (LA) 5 W 2 (AG) 3 ethanolamine (WALP16(+10))] incorporated in large unilamellar vesicles of 1,2-dimyristoyl- sn -glycero-3-phosphocholine. Both peptides consist of an alternating leucine/alanine hydrophobic core sequence flanked by tryptophan residues as interfacial anchor residues. In the case of WALP16(+10), this sequence is extended at both ends by 5-aa glycine/alanine tails extending into the aqueous phase surrounding the bilayer. H/D exchange of labile hydrogens in these peptides was monitored in time after dilution of the vesicles in buffered deuterium oxide. It was found that the peptides can be measured by direct introduction of the proteoliposome suspension into the mass spectrometer. Several distinct H/D exchange rates were observed (corresponding to half-life values varying from ≤2 to ≈2 × 10 4 min). Fast exchange rates were assigned to the water-exposed tails of WALP16(+10). For both WALP16 and WALP16(+10), intermediate exchange rates were assigned to the residues close to the membrane/water interface, and the slow exchange rates to the membrane-embedded hydrophobic core. These assignments were confirmed by results from collision-induced dissociation tandem mass spectrometry experiments, which allowed analysis of exchange of individual peptide amide linkages. This proteoliposome nanoelectrospray ionization mass spectrometry technique is shown to be an extremely sensitive and powerful tool for revealing site-specific information on peptide–membrane interactions.
Biochemical Journal, Aug 15, 2001
HAL (Le Centre pour la Communication Scientifique Directe), 2019
HAL (Le Centre pour la Communication Scientifique Directe), 2002
HAL (Le Centre pour la Communication Scientifique Directe), 2005
HAL (Le Centre pour la Communication Scientifique Directe), 2005
Biochemical Journal, Aug 8, 2001
A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega cl... more A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega class [GSTO; Board et al. 2000, J. Biol. Chem. 275, 24798–24806] has been identified in pig organs. It was found widely distributed in the different tissues investigated and especially abundant in liver and muscle. The hepatic enzyme has been purified to homogeneity by using its selective affinity for S-hexylglutathione over GSH, thus providing a simple method to isolate mammalian GSTO. The dimeric protein has a subunit molecular mass of 27328Da as measured by electrospray ionization MS. Internal peptide sequencing and complete cDNA sequencing revealed strong similarities with its human recombinant orthologue and two rodent GST-like proteins with the ability to catalyse the GSH-dependent reduction of dehydroascorbate. Additional similarities, including the presence of a specific N-terminal extension and of immunological cross-reactivity, support the results. Moreover, this gene encoding GSTO generates two organ-specific transcripts, suggesting transcriptional mechanisms with a significance that is as yet uncharacterized.
HAL (Le Centre pour la Communication Scientifique Directe), 1995
HAL (Le Centre pour la Communication Scientifique Directe), Nov 8, 2005
HAL (Le Centre pour la Communication Scientifique Directe), 2004
HAL (Le Centre pour la Communication Scientifique Directe), Jun 26, 2014
HAL (Le Centre pour la Communication Scientifique Directe), 1997
HAL (Le Centre pour la Communication Scientifique Directe), 2005
HAL (Le Centre pour la Communication Scientifique Directe), 2005
HAL (Le Centre pour la Communication Scientifique Directe), 1996
Cellular and Molecular Life Sciences, Jul 25, 2021
Analytical Biochemistry, Aug 1, 1995
Reversed-phase high-performance liquid chromatography coupled to electrospray ionization-mass spe... more Reversed-phase high-performance liquid chromatography coupled to electrospray ionization-mass spectrometry (ESI-MS) was used for the first time to determine the molecular masses of nine rat liver cytosolic glutathione S-transferase (GST) subunits. The precision of the measurements was ±3-4 mass units which, in practice, allowed discrimination between monomers differing by more than 8 Da. Mass accuracy was improved by replicates in the
HAL (Le Centre pour la Communication Scientifique Directe), Apr 22, 1995
HAL (Le Centre pour la Communication Scientifique Directe), Jan 23, 2003
HAL (Le Centre pour la Communication Scientifique Directe), May 19, 2000
HAL (Le Centre pour la Communication Scientifique Directe), 1995
A method is described to study the precise positioning of transmembrane peptides in a phospholipi... more A method is described to study the precise positioning of transmembrane peptides in a phospholipid bilayer combining hydrogen/deuterium (H/D) exchange and nanoelectrospray ionization mass spectrometry. The method was tested by using model systems consisting of designed α-helical transmembrane peptides [acetylGW 2 (LA) 5 W 2 Aethanolamine (WALP16) and acetyl-(GA) 3 W 2 (LA) 5 W 2 (AG) 3 ethanolamine (WALP16(+10))] incorporated in large unilamellar vesicles of 1,2-dimyristoyl- sn -glycero-3-phosphocholine. Both peptides consist of an alternating leucine/alanine hydrophobic core sequence flanked by tryptophan residues as interfacial anchor residues. In the case of WALP16(+10), this sequence is extended at both ends by 5-aa glycine/alanine tails extending into the aqueous phase surrounding the bilayer. H/D exchange of labile hydrogens in these peptides was monitored in time after dilution of the vesicles in buffered deuterium oxide. It was found that the peptides can be measured by direct introduction of the proteoliposome suspension into the mass spectrometer. Several distinct H/D exchange rates were observed (corresponding to half-life values varying from ≤2 to ≈2 × 10 4 min). Fast exchange rates were assigned to the water-exposed tails of WALP16(+10). For both WALP16 and WALP16(+10), intermediate exchange rates were assigned to the residues close to the membrane/water interface, and the slow exchange rates to the membrane-embedded hydrophobic core. These assignments were confirmed by results from collision-induced dissociation tandem mass spectrometry experiments, which allowed analysis of exchange of individual peptide amide linkages. This proteoliposome nanoelectrospray ionization mass spectrometry technique is shown to be an extremely sensitive and powerful tool for revealing site-specific information on peptide–membrane interactions.
Biochemical Journal, Aug 15, 2001
HAL (Le Centre pour la Communication Scientifique Directe), 2019
HAL (Le Centre pour la Communication Scientifique Directe), 2002
HAL (Le Centre pour la Communication Scientifique Directe), 2005
HAL (Le Centre pour la Communication Scientifique Directe), 2005
Biochemical Journal, Aug 8, 2001
A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega cl... more A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega class [GSTO; Board et al. 2000, J. Biol. Chem. 275, 24798–24806] has been identified in pig organs. It was found widely distributed in the different tissues investigated and especially abundant in liver and muscle. The hepatic enzyme has been purified to homogeneity by using its selective affinity for S-hexylglutathione over GSH, thus providing a simple method to isolate mammalian GSTO. The dimeric protein has a subunit molecular mass of 27328Da as measured by electrospray ionization MS. Internal peptide sequencing and complete cDNA sequencing revealed strong similarities with its human recombinant orthologue and two rodent GST-like proteins with the ability to catalyse the GSH-dependent reduction of dehydroascorbate. Additional similarities, including the presence of a specific N-terminal extension and of immunological cross-reactivity, support the results. Moreover, this gene encoding GSTO generates two organ-specific transcripts, suggesting transcriptional mechanisms with a significance that is as yet uncharacterized.
HAL (Le Centre pour la Communication Scientifique Directe), 1995
HAL (Le Centre pour la Communication Scientifique Directe), Nov 8, 2005
HAL (Le Centre pour la Communication Scientifique Directe), 2004
HAL (Le Centre pour la Communication Scientifique Directe), Jun 26, 2014
HAL (Le Centre pour la Communication Scientifique Directe), 1997
HAL (Le Centre pour la Communication Scientifique Directe), 2005
HAL (Le Centre pour la Communication Scientifique Directe), 2005
HAL (Le Centre pour la Communication Scientifique Directe), 1996
Cellular and Molecular Life Sciences, Jul 25, 2021
Analytical Biochemistry, Aug 1, 1995
Reversed-phase high-performance liquid chromatography coupled to electrospray ionization-mass spe... more Reversed-phase high-performance liquid chromatography coupled to electrospray ionization-mass spectrometry (ESI-MS) was used for the first time to determine the molecular masses of nine rat liver cytosolic glutathione S-transferase (GST) subunits. The precision of the measurements was ±3-4 mass units which, in practice, allowed discrimination between monomers differing by more than 8 Da. Mass accuracy was improved by replicates in the
HAL (Le Centre pour la Communication Scientifique Directe), Apr 22, 1995
HAL (Le Centre pour la Communication Scientifique Directe), Jan 23, 2003
HAL (Le Centre pour la Communication Scientifique Directe), May 19, 2000