Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively
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 PharmacologyProgram in Molecular Medicine
Graduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
1995-06-01Keywords
Amino Acid Sequence; Animals; Base Sequence; Bivalvia; Cloning, Molecular; DNA, Recombinant; Escherichia coli; Hemoglobins; Molecular Sequence Data; OxygenLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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/8.6.593Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32654PubMed ID
8532684Related Resources
ae974a485f413a2113503eed53cd6c53
10.1093/protein/8.6.593