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    Millipore e coli aconitase b
    Depletion of “chelatable iron pool” removes iron-sulfur clusters from recombinant <t>aconitase</t> B in E. coli cells
    E Coli Aconitase B, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli aconitase b/product/Millipore
    Average 99 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    e coli aconitase b - by Bioz Stars, 2020-09
    99/100 stars
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    Depletion of “chelatable iron pool” removes iron-sulfur clusters from recombinant aconitase B in E. coli cells

    Journal: Free radical biology & medicine

    Article Title: Iron-sulfur Proteins Are the Major Source of Protein-bound Dinitrosyl Iron Complexes Formed in Escherichia coli Cells under Nitric Oxide Stress

    doi: 10.1016/j.freeradbiomed.2011.03.005

    Figure Lengend Snippet: Depletion of “chelatable iron pool” removes iron-sulfur clusters from recombinant aconitase B in E. coli cells

    Article Snippet: The genes encoding E. coli aconitase B [ ], dihydroxyacid dehydratase (IlvD) [ ], the redox transcription factor SoxR [ ], the heat shock cognate protein HscA [ ], and the single-stranded DNA-binding protein SSB [ ] were cloned into pET28b+ (Novagen) or pBAD (Invitrogen) expression vectors as described previously [ ].

    Techniques: Recombinant

    Correlation between the amount of recombinant aconitase B and the NO-mediated formation of protein-bound DNICs in E. coli cells

    Journal: Free radical biology & medicine

    Article Title: Iron-sulfur Proteins Are the Major Source of Protein-bound Dinitrosyl Iron Complexes Formed in Escherichia coli Cells under Nitric Oxide Stress

    doi: 10.1016/j.freeradbiomed.2011.03.005

    Figure Lengend Snippet: Correlation between the amount of recombinant aconitase B and the NO-mediated formation of protein-bound DNICs in E. coli cells

    Article Snippet: The genes encoding E. coli aconitase B [ ], dihydroxyacid dehydratase (IlvD) [ ], the redox transcription factor SoxR [ ], the heat shock cognate protein HscA [ ], and the single-stranded DNA-binding protein SSB [ ] were cloned into pET28b+ (Novagen) or pBAD (Invitrogen) expression vectors as described previously [ ].

    Techniques: Recombinant

    Removal of iron-sulfur clusters in aconitase B prevents the NO-mediated formation of protein-bound DNICs in E. coli cells

    Journal: Free radical biology & medicine

    Article Title: Iron-sulfur Proteins Are the Major Source of Protein-bound Dinitrosyl Iron Complexes Formed in Escherichia coli Cells under Nitric Oxide Stress

    doi: 10.1016/j.freeradbiomed.2011.03.005

    Figure Lengend Snippet: Removal of iron-sulfur clusters in aconitase B prevents the NO-mediated formation of protein-bound DNICs in E. coli cells

    Article Snippet: The genes encoding E. coli aconitase B [ ], dihydroxyacid dehydratase (IlvD) [ ], the redox transcription factor SoxR [ ], the heat shock cognate protein HscA [ ], and the single-stranded DNA-binding protein SSB [ ] were cloned into pET28b+ (Novagen) or pBAD (Invitrogen) expression vectors as described previously [ ].

    Techniques:

    Recombinant aconitase B is modified forming protein-bound DNIC in E. coli cells under NO stress

    Journal: Free radical biology & medicine

    Article Title: Iron-sulfur Proteins Are the Major Source of Protein-bound Dinitrosyl Iron Complexes Formed in Escherichia coli Cells under Nitric Oxide Stress

    doi: 10.1016/j.freeradbiomed.2011.03.005

    Figure Lengend Snippet: Recombinant aconitase B is modified forming protein-bound DNIC in E. coli cells under NO stress

    Article Snippet: The genes encoding E. coli aconitase B [ ], dihydroxyacid dehydratase (IlvD) [ ], the redox transcription factor SoxR [ ], the heat shock cognate protein HscA [ ], and the single-stranded DNA-binding protein SSB [ ] were cloned into pET28b+ (Novagen) or pBAD (Invitrogen) expression vectors as described previously [ ].

    Techniques: Recombinant, Modification