BACTERIAL EXPRESSION OF SCAPHARCA DIMERIC HEMOGLOBIN - A SIMPLE-MODELSYSTEM FOR INVESTIGATING PROTEIN COOPERATIVITY

Recombinant Scapharca homodimeric hemoglobin has been expressed at hig h levels from a synthetic gene in Escherichia coli. Addition of the he me precursor delta-aminolevulinic acid to the expression culture resul ts 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 pro tein, like those of native hemoglobin, diffract to high resolution whi ch will allow functional studies of site-directed mutants to be correl ated with detailed structural analyses.