Human Serum Albumin Hybrid Incorporating Synthetic Hemes:A Novel O_2-Carrying Hemoprotein

Incorporation of synthetic heme (FeP) into recombinant human serum albumin(rHSA) provides an artificial hemoprotein(rHSA-FeP) which can bind and release oxygenreversibly under physiological conditions(in aqueous media, pH 7.3, 37 ℃) like hemoglobin(Hb) and myoglobin. An rHSA host absorbs maximally eight FeP molecules, and thesolution properties are almost identical to those of rHSA itself. The second-order structureand surface charge distribution of rHSA were always constant independent of the bindingnumbers of FeP. Its O2-binding ability satisfies the initial clinical requirements for red cellsubstitute. Although the NO-binding affinity is 8-fold high compared to the Hb＇s,administration of this fluid into rats showed negligible change in the blood pressure.Physiological responses to exchange transfusion with this rHSA-FeP into anaesthetized ratshave also been evaluated.