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desulfovibrio vulgaris  (DSMZ)
94
DSMZ desulfovibrio vulgaris
Fig. 1. Alignment of FrdC/SdhC sequences of sulphate-reducing bacteria, Wolinella succinogenes and Bacillus subtilis. The conserved His residues (H, supposed haem-binding sites) and the Glu (E) residues corresponding to E66 of W. succinogenes and B. subtilis, and to E180 of W. succinogenes, are boxed and outlined in black, respectively. Transmembrane helices predicted by the TMHMM program (http://www.cbs.dtu.dk/services/TMHMM) are marked in grey. The sequences were compared by CLUSTAL W in the protein database ExPASy (http://www.ebi.ac.uk/clustalw/index.html). The alignment contains 9 residues identical to all sequences, 23 conserved and 15 semiconserved substitutions according to CLUSTAL W (matrix, blosum; gap open, 1; gap extension, 0?05; end gaps, 10; other settings, default). B.s., B. subtilis (NCBI accession number CAB14805), D.v., <t>Desulfovibrio</t> <t>vulgaris</t> (AE017285); D.d., Desulfovibrio desulfuricans strains G20 (NC_007519) and Essex 6 (partial sequence; this study); D.a., Desulfobacterium autotrophicum (unpublished); D.p., Desulfotalea psychrophila (CR522870); G.s., Geobacter sulfurreducens (AE017180); W.s., W. succinogenes (CAE09943).
Desulfovibrio Vulgaris, supplied by DSMZ, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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goat polyclonal anti β1  (Cell Signaling Technology Inc)
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Fig. 1. Alignment of FrdC/SdhC sequences of sulphate-reducing bacteria, Wolinella succinogenes and Bacillus subtilis. The conserved His residues (H, supposed haem-binding sites) and the Glu (E) residues corresponding to E66 of W. succinogenes and B. subtilis, and to E180 of W. succinogenes, are boxed and outlined in black, respectively. Transmembrane helices predicted by the TMHMM program (http://www.cbs.dtu.dk/services/TMHMM) are marked in grey. The sequences were compared by CLUSTAL W in the protein database ExPASy (http://www.ebi.ac.uk/clustalw/index.html). The alignment contains 9 residues identical to all sequences, 23 conserved and 15 semiconserved substitutions according to CLUSTAL W (matrix, blosum; gap open, 1; gap extension, 0?05; end gaps, 10; other settings, default). B.s., B. subtilis (NCBI accession number CAB14805), D.v., <t>Desulfovibrio</t> <t>vulgaris</t> (AE017285); D.d., Desulfovibrio desulfuricans strains G20 (NC_007519) and Essex 6 (partial sequence; this study); D.a., Desulfobacterium autotrophicum (unpublished); D.p., Desulfotalea psychrophila (CR522870); G.s., Geobacter sulfurreducens (AE017180); W.s., W. succinogenes (CAE09943).
Goat Polyclonal Anti β1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mac valves no. 6622 valve  (MAC Valves Inc)
90
MAC Valves Inc mac valves no. 6622 valve
Fig. 1. Alignment of FrdC/SdhC sequences of sulphate-reducing bacteria, Wolinella succinogenes and Bacillus subtilis. The conserved His residues (H, supposed haem-binding sites) and the Glu (E) residues corresponding to E66 of W. succinogenes and B. subtilis, and to E180 of W. succinogenes, are boxed and outlined in black, respectively. Transmembrane helices predicted by the TMHMM program (http://www.cbs.dtu.dk/services/TMHMM) are marked in grey. The sequences were compared by CLUSTAL W in the protein database ExPASy (http://www.ebi.ac.uk/clustalw/index.html). The alignment contains 9 residues identical to all sequences, 23 conserved and 15 semiconserved substitutions according to CLUSTAL W (matrix, blosum; gap open, 1; gap extension, 0?05; end gaps, 10; other settings, default). B.s., B. subtilis (NCBI accession number CAB14805), D.v., <t>Desulfovibrio</t> <t>vulgaris</t> (AE017285); D.d., Desulfovibrio desulfuricans strains G20 (NC_007519) and Essex 6 (partial sequence; this study); D.a., Desulfobacterium autotrophicum (unpublished); D.p., Desulfotalea psychrophila (CR522870); G.s., Geobacter sulfurreducens (AE017180); W.s., W. succinogenes (CAE09943).
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β1 integrin  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology β1 integrin
Fig. 1. Alignment of FrdC/SdhC sequences of sulphate-reducing bacteria, Wolinella succinogenes and Bacillus subtilis. The conserved His residues (H, supposed haem-binding sites) and the Glu (E) residues corresponding to E66 of W. succinogenes and B. subtilis, and to E180 of W. succinogenes, are boxed and outlined in black, respectively. Transmembrane helices predicted by the TMHMM program (http://www.cbs.dtu.dk/services/TMHMM) are marked in grey. The sequences were compared by CLUSTAL W in the protein database ExPASy (http://www.ebi.ac.uk/clustalw/index.html). The alignment contains 9 residues identical to all sequences, 23 conserved and 15 semiconserved substitutions according to CLUSTAL W (matrix, blosum; gap open, 1; gap extension, 0?05; end gaps, 10; other settings, default). B.s., B. subtilis (NCBI accession number CAB14805), D.v., <t>Desulfovibrio</t> <t>vulgaris</t> (AE017285); D.d., Desulfovibrio desulfuricans strains G20 (NC_007519) and Essex 6 (partial sequence; this study); D.a., Desulfobacterium autotrophicum (unpublished); D.p., Desulfotalea psychrophila (CR522870); G.s., Geobacter sulfurreducens (AE017180); W.s., W. succinogenes (CAE09943).
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Fig. 1. Alignment of FrdC/SdhC sequences of sulphate-reducing bacteria, Wolinella succinogenes and Bacillus subtilis. The conserved His residues (H, supposed haem-binding sites) and the Glu (E) residues corresponding to E66 of W. succinogenes and B. subtilis, and to E180 of W. succinogenes, are boxed and outlined in black, respectively. Transmembrane helices predicted by the TMHMM program (http://www.cbs.dtu.dk/services/TMHMM) are marked in grey. The sequences were compared by CLUSTAL W in the protein database ExPASy (http://www.ebi.ac.uk/clustalw/index.html). The alignment contains 9 residues identical to all sequences, 23 conserved and 15 semiconserved substitutions according to CLUSTAL W (matrix, blosum; gap open, 1; gap extension, 0?05; end gaps, 10; other settings, default). B.s., B. subtilis (NCBI accession number CAB14805), D.v., Desulfovibrio vulgaris (AE017285); D.d., Desulfovibrio desulfuricans strains G20 (NC_007519) and Essex 6 (partial sequence; this study); D.a., Desulfobacterium autotrophicum (unpublished); D.p., Desulfotalea psychrophila (CR522870); G.s., Geobacter sulfurreducens (AE017180); W.s., W. succinogenes (CAE09943).

Journal: Microbiology (Reading, England)

Article Title: Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria.

doi: 10.1099/mic.0.28849-0

Figure Lengend Snippet: Fig. 1. Alignment of FrdC/SdhC sequences of sulphate-reducing bacteria, Wolinella succinogenes and Bacillus subtilis. The conserved His residues (H, supposed haem-binding sites) and the Glu (E) residues corresponding to E66 of W. succinogenes and B. subtilis, and to E180 of W. succinogenes, are boxed and outlined in black, respectively. Transmembrane helices predicted by the TMHMM program (http://www.cbs.dtu.dk/services/TMHMM) are marked in grey. The sequences were compared by CLUSTAL W in the protein database ExPASy (http://www.ebi.ac.uk/clustalw/index.html). The alignment contains 9 residues identical to all sequences, 23 conserved and 15 semiconserved substitutions according to CLUSTAL W (matrix, blosum; gap open, 1; gap extension, 0?05; end gaps, 10; other settings, default). B.s., B. subtilis (NCBI accession number CAB14805), D.v., Desulfovibrio vulgaris (AE017285); D.d., Desulfovibrio desulfuricans strains G20 (NC_007519) and Essex 6 (partial sequence; this study); D.a., Desulfobacterium autotrophicum (unpublished); D.p., Desulfotalea psychrophila (CR522870); G.s., Geobacter sulfurreducens (AE017180); W.s., W. succinogenes (CAE09943).

Article Snippet: Desulfovibrio desulfuricans (strain Essex 6, DSMZ no. 642) and Desulfovibrio vulgaris (strain Hildenborough, DSMZ no. 644) were used.

Techniques: Bacteria, Binding Assay, Sequencing

Fig. 2. Growth of D. desulfuricans (strain Essex 6) (a) and D. vulgaris (b) on fumarate (filled symbols) and sulphate (open symbols). Growth was performed under anoxic conditions in modified medium 63 containing H2+fumarate ($), formate+ fumarate (&), succinate+sulphate (%), lactate+sulphate (e) and sulphate (#) as the substrates for growth.

Journal: Microbiology (Reading, England)

Article Title: Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria.

doi: 10.1099/mic.0.28849-0

Figure Lengend Snippet: Fig. 2. Growth of D. desulfuricans (strain Essex 6) (a) and D. vulgaris (b) on fumarate (filled symbols) and sulphate (open symbols). Growth was performed under anoxic conditions in modified medium 63 containing H2+fumarate ($), formate+ fumarate (&), succinate+sulphate (%), lactate+sulphate (e) and sulphate (#) as the substrates for growth.

Article Snippet: Desulfovibrio desulfuricans (strain Essex 6, DSMZ no. 642) and Desulfovibrio vulgaris (strain Hildenborough, DSMZ no. 644) were used.

Techniques:

Fig. 3. Growth of D. desulfuricans (strain Essex 6) (a) and of D. vulgaris (b) on fumarate, and excretion of malate, succinate and acetate. The bacteria were grown ($, OD578) in modified medium 63 with 50 mM fumarate. Fumarate (m) and the end products [succinate (&), malate (n) and acetate (%)] were determined in the supernatant by HPLC.

Journal: Microbiology (Reading, England)

Article Title: Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria.

doi: 10.1099/mic.0.28849-0

Figure Lengend Snippet: Fig. 3. Growth of D. desulfuricans (strain Essex 6) (a) and of D. vulgaris (b) on fumarate, and excretion of malate, succinate and acetate. The bacteria were grown ($, OD578) in modified medium 63 with 50 mM fumarate. Fumarate (m) and the end products [succinate (&), malate (n) and acetate (%)] were determined in the supernatant by HPLC.

Article Snippet: Desulfovibrio desulfuricans (strain Essex 6, DSMZ no. 642) and Desulfovibrio vulgaris (strain Hildenborough, DSMZ no. 644) were used.

Techniques: Bacteria

Fig. 4. Succinate : DMN reductase activity of D. vulgaris and effect of the uncoupler CCCP. The activity (DMN reduction by succinate) was measured with cells of the bacteria (6?5 mg protein ml”1) by recording the reduction of DMN spectroscopi- cally at 270 nm and 290 nm (reference wavelength). CCCP (arrow) was added at 10 mM.

Journal: Microbiology (Reading, England)

Article Title: Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria.

doi: 10.1099/mic.0.28849-0

Figure Lengend Snippet: Fig. 4. Succinate : DMN reductase activity of D. vulgaris and effect of the uncoupler CCCP. The activity (DMN reduction by succinate) was measured with cells of the bacteria (6?5 mg protein ml”1) by recording the reduction of DMN spectroscopi- cally at 270 nm and 290 nm (reference wavelength). CCCP (arrow) was added at 10 mM.

Article Snippet: Desulfovibrio desulfuricans (strain Essex 6, DSMZ no. 642) and Desulfovibrio vulgaris (strain Hildenborough, DSMZ no. 644) were used.

Techniques: Activity Assay, Bacteria

Fig. 6. Unrooted bootstrapped tree of the DctP homologues from D. desulfuricans G20 (Dde proteins) and D. vulgaris (DVU proteins). The tree was obtained by analysis of the CLUSTAL X aligned sequences by

Journal: Microbiology (Reading, England)

Article Title: Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria.

doi: 10.1099/mic.0.28849-0

Figure Lengend Snippet: Fig. 6. Unrooted bootstrapped tree of the DctP homologues from D. desulfuricans G20 (Dde proteins) and D. vulgaris (DVU proteins). The tree was obtained by analysis of the CLUSTAL X aligned sequences by

Article Snippet: Desulfovibrio desulfuricans (strain Essex 6, DSMZ no. 642) and Desulfovibrio vulgaris (strain Hildenborough, DSMZ no. 644) were used.

Techniques: