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Volume 361, Issue 2-3 p. 265-268
Research letter
Free Access

DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity

Didier Belorgey

Didier Belorgey

Laboratoire d'Enzymologie, INSERM U392, Université Louis Pasteur de Strasbourg, F-67400 Illkirch, France

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Joseph G. Bieth

Corresponding Author

Joseph G. Bieth

Laboratoire d'Enzymologie, INSERM U392, Université Louis Pasteur de Strasbourg, F-67400 Illkirch, France

Corresponding author. INSERM U392, Faculté de Pharmacie, 74 route du Rhin, F-67400 Illkirch, France. Fax: (33) 88 67 92 42.Search for more papers by this author
First published: March 20, 1995
Citations: 32

Abstract

DNA binds neutrophil elastase and mucus proteinase inhibitor as evidenced by affinity chromatography on elastase-Sepharose, inhibitor-Sepharose and DNA-cellulose. DNA is a potent hyperbolic inhibitor of elastase. The polynucleotide-enzyme complex is partially active on synthetic substrates and on elastin. DNA strongly increases k diss and K i for the inhibition of elastase by mucus proteinase inhibitor. The above effects are all salt-dependent. At physiological ionic strength, DNA is a potent inhibitor of the elastolytic activity of elastase and increases k diss and K i for the elastase-mucus proteinase inhibitor interaction 160-fold and 100-fold, respectively.