ArticleJournal of fluorescence2007
Calcium ion-induced stabilization and refolding of agkisacutacin from Agkistrodon acutus venom studied by fluorescent spectroscopy.
Article in Journal of fluorescence, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Cerebrospinal Fluid of Preeclamptic and Normotensive Pregnant Women Compared to Nonpregnant Women Analyzed with Mass Spectrometry.ACS omega · 2020Article
- Oxygen-dependent oxidation of Fe(II) to Fe(III) and interaction of Fe(III) with bovine serum albumin, leading to a hysteretic effect on the fluorescence of bovine serum albumin.Journal of fluorescence · 2008Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Agkisacutacin isolated from the venom of Agkistrodon acutus is a coagulation factor IX / coagulation factor X-binding protein with marked anticoagulant- and platelet-modulating activities. Ca(2+) ion-induced stabilization and refolding of Agkisacutacin have been studied by following fluorescent measurements. Ca(2+) ions not only increase the structural stability of agkisacutacin against GdnHCl denaturation, but also induce its refolding. The GdnHCl-induced unfolding of the apo-agkisacutacin and the purified agkisacutacin is a single-step process with no detectable intermediate state. Ca(2+) ions play an important role in the stabilization of the structure of agkisacutacin. Ca(2+)-stabilized agkisacutacin exhibits higher resistance to GdnHCl denaturation than the apo-agkisacutacin. It is possible to induce refolding of the unfolded apo-agkisacutacin merely by adding 1 mM Ca(2+) ions without changing the concentration of the denaturant. The kinetic result of Ca(2+)-induced refolding provides evidences for that agkisacutacin consists of at least two refolding phases and the first phase of Ca(2+)-induced refolding should involve the formation of the compact Ca(2+)-binding site regions, and subsequently, the protein undergoes further conformational rearrangements to form the native structure.
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