Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively
AuthorsSummerford, Candace M.
Pardanani, Animesh Dev
Betts, Andrew H.
Poteete, Anthony R.
Royer, William E.
UMass Chan AffiliationsDepartment of Biochemistry and Molecular Pharmacology
Program in Molecular Medicine
Graduate School of Biomedical Sciences
KeywordsAmino Acid Sequence; Animals; Base Sequence; Bivalvia; Cloning, Molecular; DNA, Recombinant; Escherichia coli; Hemoglobins; Molecular Sequence Data; Oxygen
Medicine and Health Sciences
MetadataShow full item record
AbstractRecombinant 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.
Protein Eng. 1995 Jun;8(6):593-9.
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/32654