A Manganese Superoxide Dismutase fromSerratia marcescens

Publisher Website
Google Scholar
Abstract
Superoxide dismutase was easily isolated from Serratia marcescensATCC 21074 by ammonium sulfate fractionation and Dyemātrex Gel Green A chromatography. The purified enzyme was 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−1 cm−1 at 280 nm and 8.9×102 M−1 cm−1 at 470 nm. The enzyme showed similarities with manganese superoxide dismutases from other prokaryotes.