Abstract
Extracellular-superoxide dismutase (EC-SOD; 1.15.1.1,) 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
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References
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© 1988 Plenum Press, New York
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Marklund, S.L., Tibell, L., Hjalmarsson, K., Skogman, G., Engström, Å., Edlund, T. (1988). Sequence of Complementary DNA Encoding Human Extracellular-Superoxide Dismutase and Production of Recombinant Enzyme. In: Simic, M.G., Taylor, K.A., Ward, J.F., von Sonntag, C. (eds) Oxygen Radicals in Biology and Medicine. Basic Life Sciences, vol 49. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5568-7_107
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DOI: https://doi.org/10.1007/978-1-4684-5568-7_107
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