A Manganese Superoxide Dismutase from Serratia marcescens

概要

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Superoxide dismutase was easily isolated from Serratia marcescens ATCC 21074 by ammoniumsulfate fractionation and Dyematrex Gel Green A chromatography. The purified enzymewas a manganese-containing protein with a molecular weight of 4.8×104. Combination of gel electrophoresis in dodecylsulfate and gel filtration showed that it was composed of two equal molecular subunits. The dimeric protein contained 1.5 g atoms of manganese and exhibited molecular extinction coefficients of 9.4×104 M-1cm-1 at 280 nmand 8.9×102 M-1cm-1at 470 nm. The enzyme showed similarities with manganese superoxide dismutases from other prokaryotes.
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