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

• 出 处: 应用化学
• 发表日期: 2001年05期
• 关键词: Albumin coordinated covalently Serum viscosity hydrophobic hydrophilic ambient i

Incorporation of synthetic heme(FeP) into recombinant human serum albumin(rHSA) provides an artificial hemoprotein(rHSA-FeP) which can bind and release oxygen reversibly under physiological conditions(in aqueous media, pH 7 3, 37 ℃) like hemoglobin(Hb) and myoglobin. An rHSA host absorbs maximally eight FeP molecules, and the solution properties are almost identical to those of rHSA itself. The second-order structure and surface charge distribution of rHSA were always constant independent of the binding numbers of FeP. Its O 2-binding ability satisfies the initial clinical requirements for red cell substitute. 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 rats have also been evaluated.

Incorporation of synthetic heme (FeP) into recombinant human serum albumin (rHSA) provides an artificial hemoprotein (rHSA-FeP) which can bind and release oxygen reversibly under physiological conditions (in aqueous media, pH 7 3, 37 ° C) ) and myoglobin. An rHSA host absorbs maximally eight FeP molecules, and the solution properties are almost identical to those of rHSA itself. The second-order structure and surface charge distribution of rHSA were always constant independent of the binding numbers of FeP. Its O 2-binding wish for the initial clinical requirements for red cell substitute. 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 rats have also been evaluated.