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Concise Publication Free access | 10.1172/JCI107816

Superoxide Dismutases in Polymorphonuclear Leukocytes

Marvin L. Salin and Joe M. McCord

Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710

Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710

Find articles by Salin, M. in: PubMed | Google Scholar

Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710

Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710

Find articles by McCord, J. in: PubMed | Google Scholar

Published October 1, 1974 - More info

Published in Volume 54, Issue 4 on October 1, 1974
J Clin Invest. 1974;54(4):1005–1009. https://doi.org/10.1172/JCI107816.
© 1974 The American Society for Clinical Investigation
Published October 1, 1974 - Version history
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Abstract

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.

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