Denaturation behavior of antithrombin in guanidinium chloride. Irreversibility of unfolding caused by aggregation
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00327a033
Reference67 articles.
1. Occurrence and characterization of stable intermediate state(s) in the unfolding of ovomucoid by guanidine hydrochloride
2. Acceleration of the Reaction between, Thrombin and Antithrombin III by Non-stoichiometric Amounts of Heparin
3. Evidence by Chemical Modification for the Involvement of One or More Tryptophanyl Residues of Bovine Antithrombin in the Binding of High-Affinity Heparin
4. Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin.
5. The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin.
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