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Bothrojaracin

WebDec 1, 1998 · Bothroalternin (MW 27 kDa), a new member of the family of C-type lectins is a thrombin inhibitor which was purified from pooled B. alternatus venom by affinity chromatography on PPACK-thrombin-Sepharose, followed by size exclusion and reverse-phase on HPLC columns.

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WebOct 1, 1999 · Bothrojaracin, a 27 kDa protein isolated from Bothrops jararaca venom, forms a non-covalent complex with thrombin, thus blocking its activity. We have previously identified a bothrojaracin-like protein in B. alternatus venom [Castro, H.C., Dutra, D.L.S., Oliveira-Carvalho, A.L., Zingali, R.B., 1998. WebFeb 1, 2003 · Here, bothrojaracin (BJC), a CLP from Bothrops jararaca venom that is also a thrombin inhibitor, has been used as a model to study the subunit dissociation and unfolding of CLPs from snake venom.... オークラ輸送機 agv https://cgreentree.com

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WebSep 7, 1999 · Bothrojaracin, a 27-kDa C-type lectin from Bothrops jararaca venom, is a selective and potent thrombin inhibitor (K(d) = 0.6 nM) which interacts with the two thrombin anion-binding exosites (I and II) but not with its catalytic site. In the present study, we analyzed the allosteric effects produced … WebOct 1, 1999 · Bothrojaracin, a 27 kDa protein isolated from Bothrops jararacavenom, forms a non-covalent complex with thrombin, thus blocking its activity. We have previously identified a bothrojaracin-like protein in B. alternatusvenom [Castro, H.C., Dutra, D.L.S., Oliveira-Carvalho, A.L., Zingali, R.B., 1998. WebMay 9, 2005 · Bothrojaracin is a snake venom-derived protein that binds to thrombin exosites 1 and 2. Complex formation impairs several exosite-dependent activities of thrombin including fibrinogen cleavage and platelet activation. Bothrojaracin also interacts with proexosite 1 on prothrombin thus decreasing the zymogen activation by the … オークラ輸送機 カタログ

Subunit Dissociation, Unfolding, and Inactivation of Bothrojaracin, …

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Bothrojaracin

Bothrojaracin: A Potent Two-Site-Directed …

WebBothrojaracin is a potent and selective thrombin inhibitor that has been isolated from the venom of Bothrops jararaca. It does not interact with the catalytic site of the enzyme but binds to both ani... WebBothrojaracin is a potent and specific alpha-thrombin inhibitor (Kd approximately 0.6 nM) isolated from Bothrops jararaca venom. It binds to both of thrombin's anion-binding exosites (1 and 2), thus inhibiting the ability of the enzyme to act upon several natural macromolecular substrates, such as fibrinogen, platelet receptor, protein C, and factor V. …

Bothrojaracin

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WebJan 21, 2003 · Here, bothrojaracin (BJC), a CLP from Bothrops jararaca venom that is also a thrombin inhibitor, has been used as a model to study the subunit dissociation and unfolding of CLPs from snake venom. Dithiothreitol (DTT) up to 10 mM produces minor effects on the tertiary structure and activity of BJC. Web× Close. The Infona portal uses cookies, i.e. strings of text saved by a browser on the user's device. The portal can access those files and use them to remember the user's data, such as their chosen settings (screen view, interface language, etc.), or their login data.

WebSummary Bothrojaracin (BJC) is a 27 kDa snake venom protein from Bothrops jararaca that has been characterized as a potent ligand (K D = 75 nM) of human prothrombin (Monteiro RQ, Bock PE, Bianconi ML, Zingali RB, Protein Sci 2001; 10: 1897-904). BJC binds to the partially exposed anion-binding exosite I (proexosite I) forming a stable 1:1, … Bothrojaracin binds to the thrombin precursor, prothrombin. This interaction is calcium-independent and is prevented by heparin, suggesting that it is mediated by exosite 2. Bothrojaracin inhibits platelet activation induced by clot-bound thrombin and slowly dissociates thrombin from the fibrin clots.

WebBothrojaracin binds to the thrombin precursor, prothrombin. This interaction is calcium-independent and is prevented by heparin, suggesting that it is mediated by exosite 2. … WebIndeed, bothrojaracin and hirugen do not decrease the amidolytic activity of thrombin. However, triabin partially suppresses this activity. Since this effect is low compared to its inhibitory activity on fibrinogen clotting and platelet aggregation, it is conceivable that it binds only to the anion-binding exosite.

WebDec 31, 2008 · Bothrojaracin (BJC) is a 27-kD snake venom protein from Bothrops jararaca that has been characterized as a potent thrombin inhibitor. BJC binds to exosites I and II, with a dissociation constant...

WebOct 12, 1993 · Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom: Characterization and mechanism of thrombin inhibition Russolina B. Zingali … オークラ輸送機 dmgWebBothrojaracin (BJC) is a potent and highly specific thrombin inhibitor isolated from the venom of the jararaca snake common to Brazil (Bothrops jararaca) (Zingali et al. 1993). … pantone argentoWebSep 1, 2016 · Bothrojaracin is a 27 kDa C-type lectin-like protein from Bothrops jararaca snake venom. It behaves as a potent thrombin inhibitor upon high-affinity binding to … pantone aronaWebFeb 1, 2005 · Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = 175 nM). Incubation of BJC with human or rat plasma produced a ... オークラ輸送機 cadWebAug 20, 2010 · Bothrojaracin (BJC) is a 27-kD snake venom protein from Bothrops jararaca that has been characterized as a potent thrombin inhibitor. pantone ase filesWebMay 1, 2016 · Bothrojaracin is a 27 kDa C-type lectin-like protein from Bothrops jararaca snake venom. It behaves as a potent thrombin inhibitor upon high-affinity binding to thrombin exosites. Bothrojaracin... panto near me 2021WebMay 1, 2001 · Bothrojaracin (BJC) is a 27-kD protein from Bothrops jararaca venom that interacts with alpha-thrombin (K (D) = 0.7 nM) through both anion-binding exosites I and II. オークラ輸送機 コンベア