Purification and properties of a manganese-containing superoxide dismutase from Acholeplasma laidlawii.
From the prokaryotic microorganism Acholeplasma laidlawii the major manganese-containing superoxide dismutase has been purified to homogeneity, as judged by polyacrylamide gel electrophoresis. The molecular mass of the enzyme was found to be 41 500 Da. It consists of two subunits of identical size and has an isoelectric point of 6.4. The enzyme contains 0.51 +/- 0.05 atoms of manganese per subunit. Its amino-acid composition and light absorption spectra are presented and compared with Mn- and Fe- containing superoxide dismutases from other prokaryotic organisms.
D000128:Acholeplasma laidlawii / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D003593:Cytoplasm / Q000201:enzymology; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008345:Manganese / Q000032:analysis*; D008670:Metals / Q000032:analysis; D008970:Molecular Weight; D013482:Superoxide Dismutase / Q000032:analysis* / Q000302:isolation & purification
D000596:Amino Acids; D008670:Metals; D008345:Manganese; D013482:Superoxide Dismutase