Cm. Summerford et al., BACTERIAL EXPRESSION OF SCAPHARCA DIMERIC HEMOGLOBIN - A SIMPLE-MODELSYSTEM FOR INVESTIGATING PROTEIN COOPERATIVITY, Protein engineering, 8(6), 1995, pp. 593-599
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.