Sequence of Complementary DNA Encoding Human Extracellular-Superoxide Dismutase and Production of Recombinant Enzyme
Part of the
Basic Life Sciences
book series (BLSC, volume 49)
Extracellular-superoxide dismutase (EC-SOD; 18.104.22.168,) 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
KeywordsHeparan Sulfate Endothelial Cell Surface Synovial Fluid2 Terminal Amino Acid Sequence CuZn SODs
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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© Plenum Press, New York 1988