Porcine superoxide dismutase |
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Authors: | Marvin L Salin W W Wilson |
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Institution: | (1) Dept. of Biochemistry, Mississippi State University, 39762 Mississippi State, MS, USA;(2) Dept. of Chemistry, Mississippi State University, 39762 Mississippi State, MS, USA |
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Abstract: | Summary A cuprozinc superoxide dismutase has been isolated from pig liver. The enzyme is similar to previously described cuprozinc
superoxide dismutases in that it is a dimer of about 32 000 molecular weight consisting of approximately two equally sized
subunits, and 2 atoms of copper and two atoms of zinc per molecule. It differs, however, from previously described cuprozinc
superoxide dismutases because of its higher isoelectric point; pI 6.8 vs 4.9 for bovine enzyme. The diffusion coefficient
for the porcine enzyme was determined to be 7.53×10−7 cm2s−1, while the equivalent spherical hydrodynamic radius was computed as 28.5 ?. The enzyme was observed to undergo self-association
with time. Sulfhydryl interaction is postulated to be involved. |
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