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DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity
Author(s) -
Belorgey Didier,
Bieth Joseph G.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00173-7
Subject(s) - elastase , chemistry , neutrophil elastase , biochemistry , mucus , elastin , pancreatic elastase , dna , microbiology and biotechnology , enzyme inhibitor , enzyme , sepharose , biology , immunology , ecology , genetics , inflammation
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.