[Intracellular localization, isolation and characteristics of superoxide dismutase from Propionibacterium globosum].
From Propionibacterium globosum, superoxide dismutase (superoxide: superoxide dismutase, EC 1.15.1.1) has been isolated. As shown by polyacrylamide gel electrophoresis in native and denaturation conditions, the enzyme is a homogeneous protein with a specific activity of 3300 units/mg. In native conditions the enzyme molecular mass is 45,000 as measured by gel-filtration, and 22,000 as determined by Na-dodecyl sulphate electrophoresis. The enzyme is thermostable with pH optimum at 6.1-7.5. It has been found that superoxide dismutase of P. globosum is a membrane-independent cytoplasmic protein.
D002462:Cell Membrane / Q000201:enzymology; D002850:Chromatography, Gel; D003593:Cytoplasm / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011424:Propionibacterium / Q000201:enzymology*; D013482:Superoxide Dismutase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification*
D013482:Superoxide Dismutase
Vnutrikletochnaia lokalizatsiia, vydelenie i kharakteristika superoksiddismutazy iz Propionibacterium globosum.