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Citation: Eishun TSUCHIDA, Teruyuki KOMATSU, Yuping WU, Yubin HUANG. Human Serum Albumin Hybrid Incorporating Synthetic Hemes A Novel O₂-Carrying Hemoprotein[J]. Chinese Journal of Applied Chemistry, ;2001, 18(5): 316-321. shu

Human Serum Albumin Hybrid Incorporating Synthetic Hemes A Novel O₂-Carrying Hemoprotein

1.
Department of Polymer Chemistry, Advanced Research Institute for Science and Engineering, Waseda University, Tokyo 169-8555, Japan

Received Date: 14 February 2001
Available Online: 30 March 2001

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 O₂-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.
- human serum albumin,
- heme,
- hemoprotein,
- oxygen carrier,
- O₂-binding,
- blood substitute
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Human Serum Albumin Hybrid Incorporating Synthetic Hemes A Novel O2-Carrying Hemoprotein

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Human Serum Albumin Hybrid Incorporating Synthetic Hemes A Novel O₂-Carrying Hemoprotein