The pH Dependence of Serpin-Proteinase Complex Dissociation Reveals a Mechanism of Complex Stabilization Involving Inactive and Active Conformational States of the Proteinase Which Are Perturbable by Calcium
Open Access
- 1 August 2001
- journal article
- Published by Elsevier
- Vol. 276 (35) , 32446-32455
- https://doi.org/10.1074/jbc.m104731200
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- An Ester Bond Linking a Fragment of a Serine Proteinase to Its Serpin InhibitorBiochemistry, 1998
- Role of the P6−P3‘ Region of the Serpin Reactive Loop in the Formation and Breakdown of the Inhibitory ComplexBiochemistry, 1997
- Role of the Catalytic Serine in the Interactions of Serine Proteinases with Protein Inhibitors of the Serpin FamilyPublished by Elsevier ,1995
- The Inhibition Mechanism of SerpinsPublished by Elsevier ,1995
- Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme IntermediatesPublished by Elsevier ,1995
- Kinetic Characterization of the Proteinase Binding Defect in a Reactive Site Variant of the Serpin, AntithrombinPublished by Elsevier ,1995
- A Fluorescent Probe Study of Plasminogen Activator Inhibitor-1Published by Elsevier ,1995
- Immunologic evidence for insertion of the reactive-bond loop of antithrombin into the A .beta.-sheet of the inhibitor during trapping of target proteinasesBiochemistry, 1993
- Conformational stability of the covalent complex between elastase and α1-proteinase inhibitorArchives of Biochemistry and Biophysics, 1991
- Properties of antithrombin-thrombin complex formed in the presence and in the absence of heparinBiochemical Journal, 1983