[Purification and study of two superoxide dismutases of the mushroom Pleurotus olearius].
Two different superoxide dismutases have been purified from the luminous fungus Pleurotus olearius. The second enzyme SODm presents structural differences with the first enzyme SODc previously described [5]: it has a molecular weight of 78,000 and is composed of identical subunits (20,000); it contains also two functional Mn atoms. Using an antiserum prepared against SODc, we have shown that there is no cross-reaction between these two proteins. Spectral studies of the first enzyme SODc suggest that the active center contains trivalent manganese Mn-III.
D000363:Agaricales / Q000201:enzymology*; D001487:Basidiomycota / Q000201:enzymology*; D002499:Centrifugation, Density Gradient; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D003956:Dialysis; D004591:Electrophoresis, Polyacrylamide Gel; D007501:Iron / Q000378:metabolism; D007527:Isoenzymes / Q000276:immunology / Q000302:isolation & purification; D008345:Manganese / Q000378:metabolism; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry; D013482:Superoxide Dismutase / Q000302:isolation & purification* / Q000378:metabolism
D007527:Isoenzymes; D008345:Manganese; D007501:Iron; D013482:Superoxide Dismutase
Purification et étude des deux superoxyde dismutases du champignon Pleurotus olearius