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    Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively

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    Authors
    Summerford, Candace M.
    Pardanani, Animesh Dev
    Betts, Andrew H.
    Poteete, Anthony R.
    Colotti, Gianni
    Royer, William E.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Program in Molecular Medicine
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1995-06-01
    Keywords
    Amino Acid Sequence; Animals; Base Sequence; Bivalvia; Cloning, Molecular; DNA, Recombinant; Escherichia coli; Hemoglobins; Molecular Sequence Data; Oxygen
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    https://doi.org/10.1093/protein/8.6.593
    Abstract
    Recombinant Scapharca homodimeric hemoglobin has been expressed at high levels from a synthetic gene in Escherichia coli. Addition of the heme precursor delta-aminolevulinic acid to the expression culture results in a considerable increase in the yield of soluble hemoglobin. The recombinant hemoglobin exhibits cooperative oxygen binding properties indistinguishable from native protein. Crystals of the recombinant protein, like those of native hemoglobin, diffract to high resolution which will allow functional studies of site-directed mutants to be correlated with detailed structural analyses.
    Source

    Protein Eng. 1995 Jun;8(6):593-9.

    DOI
    10.1093/protein/8.6.593
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32654
    PubMed ID
    8532684
    Related Resources

    Link to Article in PubMed

    ae974a485f413a2113503eed53cd6c53
    10.1093/protein/8.6.593
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    Morningside GSBS Scholarly Publications

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