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Recombinant human Hb-SOD fusion proteins

Grey, Marie LU ; Ratanasopa, Khuanpiroon LU and Bülow, Leif LU (2014) p.349-358
Abstract
Hemoglobin (Hb) can produce reactive oxygen species, including
superoxide anions, which are intrinsically toxic. Superoxide dismutase
(SOD) is present in red blood cells (RBCs) and provides important
protection against such oxidative stress. Upon hemolysis, Hb becomes
released from the RBCs and the normal protection systems involving SOD
and catalase become very inefficient. In these instances, both the Hb
protein in itself and its cellular surroundings may be exposed to severe
oxidative damage. In order to generate less toxic Hb variants, we have
produced fusion proteins between SOD and HbA. The fusion protein has
been prepared by coexpressing the human Hb α-chain linked to the
manganese... (More)
Hemoglobin (Hb) can produce reactive oxygen species, including
superoxide anions, which are intrinsically toxic. Superoxide dismutase
(SOD) is present in red blood cells (RBCs) and provides important
protection against such oxidative stress. Upon hemolysis, Hb becomes
released from the RBCs and the normal protection systems involving SOD
and catalase become very inefficient. In these instances, both the Hb
protein in itself and its cellular surroundings may be exposed to severe
oxidative damage. In order to generate less toxic Hb variants, we have
produced fusion proteins between SOD and HbA. The fusion protein has
been prepared by coexpressing the human Hb α-chain linked to the
manganese SOD gene as a chimeric construct together with the native
β-chain Hb gene in Eschericia coli. The engineered SOD-Hb fusion
protein retains the oxygen-binding capacity and, moreover, decreases
cytotoxic ferrylHb (HbFe(4 +)) formation when exposed to superoxide
radicals. The SOD-Hb fusion protein is also substantially less prone to
autoxidation. Our findings not only provide insight into the synergistic
functions between SOD and Hb when they are closely and spatially
organized, but could also potentially be used to develop therapeutic
blood substitutes with more efficient oxygen carrying capabilities. (Less)
Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
host publication
Hemoglobin-Based Oxygen Carriers as Red Cell Substitutes and Oxygen Therapeutics
editor
Won Kim, Hae and Gerson Greenburg, A.
edition
1
pages
10 pages
publisher
Springer
external identifiers
  • scopus:84930326874
ISBN
3642407161
978-3-642-40716-1
978-3-662-50807-7
978-3-642-40717-8
DOI
10.1007/978-3-642-40717-8_19
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2013 Springer-Verlag Berlin Heidelberg. All rights reserved.
id
1d6b4c30-12df-4536-91a1-25e254c35d1a
date added to LUP
2026-05-06 07:22:32
date last changed
2026-05-06 09:34:52
@inbook{1d6b4c30-12df-4536-91a1-25e254c35d1a,
  abstract     = {{Hemoglobin (Hb) can produce reactive oxygen species, including <br>
superoxide anions, which are intrinsically toxic. Superoxide dismutase <br>
(SOD) is present in red blood cells (RBCs) and provides important <br>
protection against such oxidative stress. Upon hemolysis, Hb becomes <br>
released from the RBCs and the normal protection systems involving SOD <br>
and catalase become very inefficient. In these instances, both the Hb <br>
protein in itself and its cellular surroundings may be exposed to severe<br>
 oxidative damage. In order to generate less toxic Hb variants, we have <br>
produced fusion proteins between SOD and HbA. The fusion protein has <br>
been prepared by coexpressing the human Hb α-chain linked to the <br>
manganese SOD gene as a chimeric construct together with the native <br>
β-chain Hb gene in <i>Eschericia coli</i>. The engineered SOD-Hb fusion <br>
protein retains the oxygen-binding capacity and, moreover, decreases <br>
cytotoxic ferrylHb (HbFe(4 +)) formation when exposed to superoxide <br>
radicals. The SOD-Hb fusion protein is also substantially less prone to <br>
autoxidation. Our findings not only provide insight into the synergistic<br>
 functions between SOD and Hb when they are closely and spatially <br>
organized, but could also potentially be used to develop therapeutic <br>
blood substitutes with more efficient oxygen carrying capabilities.}},
  author       = {{Grey, Marie and Ratanasopa, Khuanpiroon and Bülow, Leif}},
  booktitle    = {{Hemoglobin-Based Oxygen Carriers as Red Cell Substitutes and Oxygen Therapeutics}},
  editor       = {{Won Kim, Hae and Gerson Greenburg, A.}},
  isbn         = {{3642407161}},
  language     = {{eng}},
  month        = {{10}},
  pages        = {{349--358}},
  publisher    = {{Springer}},
  title        = {{Recombinant human Hb-SOD fusion proteins}},
  url          = {{http://dx.doi.org/10.1007/978-3-642-40717-8_19}},
  doi          = {{10.1007/978-3-642-40717-8_19}},
  year         = {{2014}},
}