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Inactivation of α1-proteinase inhibitor by Cu(II) and hydrogen peroxide

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Abstract

When α1-proteinase inhibitor was treated with 1–5 μM CuSO4 in the presence of H2O2 (250–1000 μM), its elastase inhibitory capacity was markedly decreased. Several other metal ions tested had either very little or no effect. The Cu(II)-catalyzed decrease in the inhibition of elastase activity can also be demonstrated in dialyzed plasma. These results are consistent with the hypothesis that in several pathological conditions in which extracellular copper levels are elevated, Cu(II)-catalyzed peroxidation of α1-proteinase inhibitor may occur at sites of inflammation where H2O2 is secreted as a major product by activated phagocytes.

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  1. Department of Biochemistry, State University of New York Health Science Center at Brooklyn, 11203, Brooklyn, N.Y., USA

    N. S. Kwon, P. C. Chan & L. Kesner

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  1. N. S. Kwon
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  2. P. C. Chan
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  3. L. Kesner
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Kwon, N.S., Chan, P.C. & Kesner, L. Inactivation of α1-proteinase inhibitor by Cu(II) and hydrogen peroxide. Agents and Actions 29, 388–393 (1990). https://doi.org/10.1007/BF01966473

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  • DOI: https://doi.org/10.1007/BF01966473

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