title: Studies on the nature of superoxide dismutase activity in sheep liver subcellular fractions.
abstract: In the absence or in the presence of 10(-4)M EDTA cytosolic and lysosomal CuZnSOD and MnSOD activities were differentiated as enzymatic and nonenzymatic (SOD-like). Both activities were about three times lower in mitochondrial matrix compared to those in cytosol and lysosomes. The cytosolic and lysosomal CuZnSOD showed an equal electrophoretic pattern: three peaks of SOD activity with Rf values of 1 = 0.10 and 0.12; 2 = 0.16 and 0.18; 3 = 0.21 and 0.22, respectively. The low anodic mobility was explained by the high isoelectric points (pI) of the three CuZnSOD isoenzymes (approximately 5.7, approximately 6.5 and approximately 7.5) contained both in cytosol and in lysosomes.
authors.affiliation: Institute of Physiology, Bulgarian Academy of Sciences, Sofia.
authors.forename: S G
authors.initials: SG
authors.lastname: Konstantinova
authors.forename: E M
authors.initials: EM
authors.lastname: Russanov
mesh_terms: D000818:Animals; D003594:Cytoplasmic Granules / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D012756:Sheep; D013347:Subcellular Fractions / Q000201:enzymology*; D013482:Superoxide Dismutase / Q000378:metabolism*
chemical_list: D007527:Isoenzymes; D013482:Superoxide Dismutase