Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively
Graduate School of Biomedical Sciences; Program in Molecular Medicine; Department of Biochemistry and Molecular Pharmacology
Medical Subject Headings
Amino Acid Sequence; Animals; Base Sequence; Bivalvia; Cloning, Molecular; DNA, Recombinant; Escherichia coli; Hemoglobins; Molecular Sequence Data; Oxygen
Life Sciences | Medicine and Health Sciences
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.
Rights and Permissions
Citation: Protein Eng. 1995 Jun;8(6):593-9.
Summerford, Candace M.; Pardanani, Animesh Dev; Betts, Andrew H.; Poteete, Anthony R.; Colotti, Gianni; and Royer, William E., "Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively" (1995). GSBS Student Publications. 1213.