Sequence of Complementary DNA Encoding Human Extracellular-Superoxide Dismutase and Production of Recombinant Enzyme

  • Stefan L. Marklund
  • Lena Tibell
  • Karin Hjalmarsson
  • Gunnar Skogman
  • Åke Engström
  • Thomas Edlund
Part of the Basic Life Sciences book series (BLSC, volume 49)


Extracellular-superoxide dismutase (EC-SOD;,) is the major SOD isoenzyme in extra- cellular fluids such as plasma, lymph1 and synovial fluid2 but also occurs in tissues.3,4 EC-SOD is heterogenous with regard to binding to Heparin-Sepharose and can be separated into three fractions: A, without affinity; B with weak affinity; and C, with relatively high affinity.5 Most EC-SOD in the vascular system apparently is bound to endothelial cell surfaces.6 Membrane-bound heparan sulfate is the likely receptor for the enzyme, and EC-SOD fraction C is the form that binds.6 EC-SOD is a tetrameric glycoprotein with an apparent subunit molecular weight of around 3 0 kDa.5 Like the CuZn SOD’s, EC-SOD contains one Cu and one Zn atom per subunit.5 Still, despite the similarities, the amino acid compositions of human CuZn SOD and EC-SOD are clearly different,5 and no cross-reaction between polyclonal rabbit antibodies directed towards the enzymes have been observed.7


Heparan Sulfate Endothelial Cell Surface Synovial Fluid2 Terminal Amino Acid Sequence CuZn SODs 
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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Stefan L. Marklund
    • 1
  • Lena Tibell
    • 2
  • Karin Hjalmarsson
    • 2
  • Gunnar Skogman
    • 2
  • Åke Engström
    • 3
  • Thomas Edlund
    • 4
  1. 1.Department of Clinical ChemistryUmeå University HospitalUmeåSweden
  2. 2.Department of Molecular Genetics and Cell BiologySYMBICOM ABUmeåSweden
  3. 3.Department of ImmunologyBiomedical CenterUppsalaSweden
  4. 4.Department of MicrobiologyUniversity of UmeåUmeåSweden

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