Hemoglobin-albumin crosslinked copolymers: reduced prooxidant reactivity

Artif Cells Blood Substit Immobil Biotechnol. 2011 Oct;39(5):293-7. doi: 10.3109/10731199.2011.563362. Epub 2011 May 31.

Abstract

We have previously reported that derivatization of hemoglobin with periodate-modified sugar derivatives such as oxidized adenosine triphosphate (oATP) leads to an increase in prooxidant reactivity at the heme. Here, we report that copolymerization of hemoglobin with serum albumin alleviates this problem completely, to the extent where the copolymer even has a slightly lower autooxidation rate compared to native hemoglobin. A similar, although not as potent, effect is obtained when hemoglobin is derivatized with oATP in the presence of small-molecule antioxidants instead of albumin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives
  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Antioxidants* / chemistry
  • Antioxidants* / metabolism
  • Blood Substitutes / chemistry
  • Blood Substitutes / metabolism*
  • Borohydrides / chemistry
  • Cross-Linking Reagents / chemistry
  • Electron Spin Resonance Spectroscopy
  • Electrophoresis, Polyacrylamide Gel
  • Heme / chemistry
  • Heme / metabolism*
  • Hemoglobins / chemistry
  • Hemoglobins / metabolism*
  • Humans
  • Oxidation-Reduction
  • Polymerization
  • Reactive Oxygen Species / metabolism
  • Serum Albumin* / chemistry
  • Serum Albumin* / metabolism
  • Spectrum Analysis

Substances

  • Antioxidants
  • Blood Substitutes
  • Borohydrides
  • Cross-Linking Reagents
  • Hemoglobins
  • Reactive Oxygen Species
  • Serum Albumin
  • Heme
  • sodium borohydride
  • Adenosine Triphosphate