Isolated human polymorphonuclear leukocytes were found to contain two distinct superoxide dismutases, electrophoretically identical to the superoxide dismutases found in other human tissues. One is inhibited by cyanide and is located in the cytosol. The other is not inhibited by cyanide and is mitochondrial. These findings disagree with reports by other laboratories, which did not find the cyanide-sensitive cytoplasmic enzyme. The superoxide dismutase-containing preparation of leukocytes released large amounts of superoxide into the medium when the cells were phagocytizing, suggesting that, if the cell population is homogeneous, superoxide production probably takes place on the outer surface of the cell membrane, in addition to inside the phagocytic vacuole.
Marvin L. Salin, Joe M. McCord
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Title and authors | Publication | Year |
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Cu,Zn superoxide dismutase and copper deprivation and toxicity in Saccharomyces cerevisiae
MA Greco, DI Hrab, W Magner, DJ Kosman |
Journal of bacteriology | 1990 |
Cytosolic copper-binding proteins in rat and mouse hepatocytes incubated continuously with Cu(II)
FA Palida, A Mas, L Arola, K Bethin, PA Lonergan, MJ Ettinger |
Biochemical Journal | 1990 |
Nippostrongylus brasiliensis and Ascaridia galli: Characterization of peroxisomes
TA Paget, M Fry, D Lloyd |
Experimental Parasitology | 1990 |
Effect of polymorphonuclear leukocyte-derived oxygen free radicals and hypochlorous acid on cardiac function and some biochemical parameters
K Prasad, J Kalra, AK Chaudhary, D Debnath |
American Heart Journal | 1990 |