NDLI: Ca(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus

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Ca(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus

Content Provider	PubMed Central
Author	Xu, Xiaolong Liu, Qingliang Yu, Huaming Xie, Yongshu
Abstract	Anticoagulation factor I (ACF I) isolated from the venom of Agkistrodon acutus is an activated coagulation factor X-binding protein in a Ca2+-dependent fashion with marked anticoagulant activity. The equilibrium unfolding/refolding of apo-ACF I, holo-ACF I, and Tb3+-reconstituted ACF I in guanidine hydrochloride (GdnHCl) solutions was studied by following the fluorescence and circular dichroism. Metal ions were found to increase the structural stability of ACF I against GdnHCl and thermal denaturation and, furthermore, influence its unfolding/refolding behavior. The GdnHCl-induced unfolding/refolding of both apo-ACF I and Tb3+-ACF I is a two-state process with no detectable intermediate state(s), whereas the GdnHCl-induced unfolding/refolding of holo-ACF I in the presence of 1 mM Ca2+ follows a three-step transition, with intermediate state a (Ia) and intermediate state b (Ib). Ca2+ ions play an important role in the stabilization of the Ia and Ib states. The decalcification of holo-ACF I shifts the ending zone of unfolding/refolding curve toward lower GdnHCl concentration, whereas the reconstitution of apo-ACF I with Tb3+ ions shifts the initial zone of denaturation curve toward higher GdnHCl concentration. Therefore, it is possible to find a denaturant concentration (2.0 M GdnHCl) at which refolding from the fully denatured state of apo-ACF I to the Ib state of holo-ACF I or to the native state of Tb3+-ACF I can be initiated merely by adding the 1 mM Ca2+ ions or 10 μM Tb3+ ions to the unfolded state of apo-ACF I, respectively, without changing the concentration of the denaturant. Using Tb3+ as a fluorescence probe of Ca2+, the kinetic results of metal ions–induced refolding provide evidence that the compact Tb3+-binding region forms first, and subsequently, the protein undergoes further conformational rearrangements to form the native structure.
Related Links	http://dx.doi.org/10.1110/ps.4130102
Ending Page	956
Page Count	13
Starting Page	944
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	4
Volume Number	11
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2002-04-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Ca(II)- and Tb(III)-induced stabilization and refolding of anticoagulation factor I from the venom of Agkistrodon acutus

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