THE BIOSYNTHESIS OF HEMOGLOBIN FROM IRON, PROTOPORPHYRIN AND GLOBIN*†

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Abstract
Formation of hemoglobin from iron, protoporphyrin and globin was studied in a chicken hemolysate system. Heme synthesis was measured as % incorporation of added radioiron into heme. The heme synthetase enzyme system was purified several hundred fold. An acetone powder of a purified enzyme preparation was stable for 4.5 months at 5[degree]C. A factor present in the supernatant solution (Fraction n) from a chicken or human hemolysate was required for maximal incorporation of the radioiron into the heme. The factor present in Fraction II could be replaced by optimal concentrations of chicken globin. A similar effect was observed with human globin. The end-product of the reaction, as characterized by electrophoresis and chromatography, was hemoglobin.