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A superoxide dismutase-human hemoglobin fusion protein showing enhanced antioxidative properties.

Grey, Marie LU ; Yainoy, Sakda LU ; Prachayasittikul, Virapong and Bülow, Leif LU (2009) In The FEBS Journal 276(21). p.6195-6203
Abstract
Much of the toxicity of Hb has been linked to its redox activity; Hb may generate reactive oxygen species, such as the superoxide anion. Superoxide is intrinsically toxic, and superoxide dismutase (SOD) provides important cellular protection. However, if the Hb molecule is located outside the red blood cell, the normal protection systems involving SOD and catalase are no longer closely associated with it, exposing Hb and its cellular surroundings to oxidative damage. In order to produce less toxic Hb molecules, we have explored gene fusion to obtain homogeneous SOD-Hb conjugates. The chimeric protein was generated by coexpressing the human Hb alpha-chain/manganese SOD gene together with the beta-chain gene in Escherichia coli. We show that... (More)
Much of the toxicity of Hb has been linked to its redox activity; Hb may generate reactive oxygen species, such as the superoxide anion. Superoxide is intrinsically toxic, and superoxide dismutase (SOD) provides important cellular protection. However, if the Hb molecule is located outside the red blood cell, the normal protection systems involving SOD and catalase are no longer closely associated with it, exposing Hb and its cellular surroundings to oxidative damage. In order to produce less toxic Hb molecules, we have explored gene fusion to obtain homogeneous SOD-Hb conjugates. The chimeric protein was generated by coexpressing the human Hb alpha-chain/manganese SOD gene together with the beta-chain gene in Escherichia coli. We show that the engineered SOD-Hb fusion protein retains the oxygen-binding capacity and, moreover, decreases cytotoxic ferrylHb (HbFe(4+)) formation when challenged with superoxide radicals. The SOD-Hb fusion protein also exhibits a 44% lower autoxidation rate and higher thermal stability than Hb alone. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
keywords
Recombinant Fusion Proteins: chemistry, Antioxidants: chemistry, Hemoglobins: chemistry, Superoxide Dismutase: chemistry
in
The FEBS Journal
volume
276
issue
21
pages
6195 - 6203
publisher
Federation of European Neuroscience Societies and Blackwell Publishing Ltd
external identifiers
  • wos:000270649500014
  • pmid:19788422
  • scopus:70349954876
ISSN
1742-464X
DOI
10.1111/j.1742-4658.2009.07323.x
language
English
LU publication?
yes
id
f9c338d6-f953-4378-b761-ef269960835c (old id 1500914)
date added to LUP
2009-12-01 10:12:52
date last changed
2017-03-05 03:42:07
@article{f9c338d6-f953-4378-b761-ef269960835c,
  abstract     = {Much of the toxicity of Hb has been linked to its redox activity; Hb may generate reactive oxygen species, such as the superoxide anion. Superoxide is intrinsically toxic, and superoxide dismutase (SOD) provides important cellular protection. However, if the Hb molecule is located outside the red blood cell, the normal protection systems involving SOD and catalase are no longer closely associated with it, exposing Hb and its cellular surroundings to oxidative damage. In order to produce less toxic Hb molecules, we have explored gene fusion to obtain homogeneous SOD-Hb conjugates. The chimeric protein was generated by coexpressing the human Hb alpha-chain/manganese SOD gene together with the beta-chain gene in Escherichia coli. We show that the engineered SOD-Hb fusion protein retains the oxygen-binding capacity and, moreover, decreases cytotoxic ferrylHb (HbFe(4+)) formation when challenged with superoxide radicals. The SOD-Hb fusion protein also exhibits a 44% lower autoxidation rate and higher thermal stability than Hb alone.},
  author       = {Grey, Marie and Yainoy, Sakda and Prachayasittikul, Virapong and Bülow, Leif},
  issn         = {1742-464X},
  keyword      = {Recombinant Fusion Proteins: chemistry,Antioxidants: chemistry,Hemoglobins: chemistry,Superoxide Dismutase: chemistry},
  language     = {eng},
  number       = {21},
  pages        = {6195--6203},
  publisher    = {Federation of European Neuroscience Societies and Blackwell Publishing Ltd},
  series       = {The FEBS Journal},
  title        = {A superoxide dismutase-human hemoglobin fusion protein showing enhanced antioxidative properties.},
  url          = {http://dx.doi.org/10.1111/j.1742-4658.2009.07323.x},
  volume       = {276},
  year         = {2009},
}