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

FEBS Letters

Belorgey, Didier¹  Bieth, Joseph G.¹ 

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

关键词: Elastase;    Mucus proteinase inhibitor;    Enzyme kinetics;    DNA;    Cystic fibrosis;    NE;    neutrophil elastase;    MPI;    mucus proteinase inhibitor = secretory leucoprotease inhibitor (SLPI);    Suc-Ala3-pNA;    succinyl-Ala3-p-nitroanilide;    MeOSuc-Ala2-Pro-Val-pNA;    methoxysuccinyl-Ala2-Pro-Val-p-nitroanilide;    RBB-elastin;    remazol Brilliant-blue elastin;   

DOI  :  10.1016/0014-5793(95)00173-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown