Abstract
The cDNA coding for a human embryonic globin protein has been obtained from an erythroleukaemic cell line. A plasmid expression system for human embryonic haemoglobin Gower II containing cDNA copies of the appropriate pair of globin genes coupled to synthetic galactose-regulated hybrid promoters has been engineered. Transformation of Saccharomyces cerevisiae with this plasmid yields a cellular system capable of high-level production of fully functional tetrameric embryonic haemoglobin. We have developed a purification scheme which gives high yields of pure human embryonic haemoglobin suitable for structural and functional studies. Preliminary characterization studies are reported.
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