2d cardiac performance analysis, image arena Search Results


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Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
Image Analysis Software Dipp Motion V/2d, supplied by DITECT Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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PhaseTech Spectroscopy 2d spectrometers
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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PHORETIX INTERNATIONAL LIMITED 2d gel analysis software phoretix 2005
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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Representative <t>2-D</t> gel showing protein spots selected for identification. Nine canalicular multispecific organic ion transporter/multidrug resistance–associated protein 2, 14 intermediate filament protein, 18 α-enolase, 21 bifunctional P-450/NADPH-P450 reductase, 22 canalicular multispecific organic ion transporter/multidrug resistance–associated protein 2, 30 ubiquitin-40S ribosomal protein, 36 intermediate filament protein, 45 glucose-6-phosphate 1-dehydrogenase, 64 glycine-tRNA ligase β subunit, 69 14-3-3 protein β subunit, 74 gasdermin, 80 fructose bisphosphate aldolase, 82 Tubulin β-1 chain, 89 vacuolar membrane–associated protein IML1, 95 tropomyosin α-1 chain/β chain, 101 tropomyosin α-3 chain, 111 glucose-6-phosphate 1-dehydrogenase, 123 ABC transporter G family member. 2-D, <t>2-dimensional</t>
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Image Search Results


Comparative 2D gel electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.

Journal:

Article Title: Involvement of Superoxide Dismutases in the Response of Escherichia coli to Selenium Oxides

doi: 10.1128/JB.184.6.1556-1564.2002

Figure Lengend Snippet: Comparative 2D gel electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.

Article Snippet: The spots on the radioactive gels were recorded by PhosphorImager technology (Molecular Dynamics) and analyzed with a 2D gel analysis software (MelanieII; Bio-Rad).

Techniques: Two-Dimensional Gel Electrophoresis, Electrophoresis, Labeling, Mass Spectrometry

Representative 2-D gel showing protein spots selected for identification. Nine canalicular multispecific organic ion transporter/multidrug resistance–associated protein 2, 14 intermediate filament protein, 18 α-enolase, 21 bifunctional P-450/NADPH-P450 reductase, 22 canalicular multispecific organic ion transporter/multidrug resistance–associated protein 2, 30 ubiquitin-40S ribosomal protein, 36 intermediate filament protein, 45 glucose-6-phosphate 1-dehydrogenase, 64 glycine-tRNA ligase β subunit, 69 14-3-3 protein β subunit, 74 gasdermin, 80 fructose bisphosphate aldolase, 82 Tubulin β-1 chain, 89 vacuolar membrane–associated protein IML1, 95 tropomyosin α-1 chain/β chain, 101 tropomyosin α-3 chain, 111 glucose-6-phosphate 1-dehydrogenase, 123 ABC transporter G family member. 2-D, 2-dimensional

Journal: Dose-Response

Article Title: Biological Entanglement–Like Effect After Communication of Fish Prior to X-Ray Exposure

doi: 10.1177/1559325817750067

Figure Lengend Snippet: Representative 2-D gel showing protein spots selected for identification. Nine canalicular multispecific organic ion transporter/multidrug resistance–associated protein 2, 14 intermediate filament protein, 18 α-enolase, 21 bifunctional P-450/NADPH-P450 reductase, 22 canalicular multispecific organic ion transporter/multidrug resistance–associated protein 2, 30 ubiquitin-40S ribosomal protein, 36 intermediate filament protein, 45 glucose-6-phosphate 1-dehydrogenase, 64 glycine-tRNA ligase β subunit, 69 14-3-3 protein β subunit, 74 gasdermin, 80 fructose bisphosphate aldolase, 82 Tubulin β-1 chain, 89 vacuolar membrane–associated protein IML1, 95 tropomyosin α-1 chain/β chain, 101 tropomyosin α-3 chain, 111 glucose-6-phosphate 1-dehydrogenase, 123 ABC transporter G family member. 2-D, 2-dimensional

Article Snippet: Gel image analysis was carried out using the Phoretix 2-D software (Progenesis PG200, Phoretix International, United Kingdom) with protein expression being quantitatively expressed as “normalized spot volume,” a parameter which combines the spot size and intensity.

Techniques: