17 research outputs found
Les Ă©lastases
Les élastases sont des protéases capables de solubiliser l’élastine fibreuse. Elles peuvent faire partie de la classe des sérine protéases, des cystéine protéases ou des métalloprotéases. Les élastases de mammifères se rencontrent principalement dans le pancréas et les phagocytes. Parmi les élastases de non-mammifères, on note une grande diversité de métalloélastases et de sérine élastases bactériennes. L’activité élastolytique varie fortement d’une élastase à l’autre et n’est, en général, pas corrélée au pouvoir catalytique de ces protéases. On peut mesurer cette activité avec de l’élastine native ou marquée. Avec des élastases pures, on peut utiliser des substrats synthétiques spécifiques. Il existe un grand nombre d’inhibiteurs naturels (protéiques) et synthétiques des élastases. Les élastases peuvent jouer un rôle pathologique dans l’emphysème pulmonaire, la mucoviscidose, l’infection, l’inflammation et l’athérosclérose
Effect of Polynucleotides on the Inhibition of Neutrophil Elastase by Mucus Proteinase Inhibitor and α 1
NMR and enzymatic investigation of the interaction between elastase and sodium trifluoroacetate
Conformational change in elastase following complexation with alpha1-proteinase inhibitor: a CD investigation.
The CD spectrum of porcine pancreatic elastase in complex with alpha1-proteinase inhibitor (alpha1-PI) was calculated by subtracting the CD spectrum of the proteolytically cleaved inhibitor from that of the elastase-alpha1-PI complex. Elastase undergoes a moderate secondary structure change: its beta-structure is partially disordered while its alpha-helix content is poorly affected. In contrast, its tertiary structure undergoes a significant structural loosening upon complexation. These alterations have been compared with those following chemical and thermal unfolding of free elastase. Inhibitor-bound elastase and the denaturation intermediate of free elastase share secondary but not tertiary structural features. On the other hand, both free and complexed elastases undergo a single-step transition in tertiary structure upon thermal unfolding. These data are discussed in terms of the inhibition and structural modification of elastase induced by alpha1-PI observed by previous investigators
Heparin accelerates the inhibition of cathepsin G by mucus proteinase inhibitor: potent effect of O-butyrylated heparin
Mapping the Suramin-Binding Sites of Human Neutrophil Elastase: Investigation by Fluorescence Resonance Energy Transfer and Molecular Modeling â€
Thermodynamic Investigation of the Heparin-Mucus Proteinase Inhibitor Binding
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