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Biochemical, pharmacological and structural characterization of BmooMP-I, a new P–I metalloproteinase from Bothrops moojeni venom
(2020-12-01)
Snakebite envenoming is still a worrying health problem in countries under development, being recognized as a neglected disease by the World Health Organization. In Latin America, snakes from the genus Bothrops are widely ...
Biochemical and enzymatic characterization of BpMP-I, a fibrinogenolytic metalloproteinase isolated from Bothropoides pauloensis snake venom
(ELSEVIER SCIENCE INCNEW YORK, 2012)
Snake Venom Metalloproteinases (SVMPs) are the most abundant components present in Viperidae venom. They are important in the induction of systemic alterations and local tissue damage after envenomation. In the present ...
Detection and characterization of metalloproteinases with gelatinolytic, fibronectinolytic and fibrinogenolytic activities in Brown spider (Loxosceles intermedia) venom
(Pergamon-elsevier Science LtdOxfordInglaterra, 1998)
Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom
(PERGAMON-ELSEVIER SCIENCE LTD, 2008)
A proteinase, named BmooMP alpha-I, from the venom of Bothrops moojeni, was purified by DEAE-Sephacel, Sephadex G-75 and heparin-agarose column chromatography. The enzyme was purified to homogeneity as judged by its migration ...
Isolation and characterization of moojenin, an acid-active, anticoagulant metalloproteinase from Bothrops moojeni venom
(PERGAMON-ELSEVIER SCIENCE LTDOXFORD, 2012)
A fibrinogenolytic metalloproteinase from Bothrops moojeni venom, named moojenin, was purified by a combination of ion-exchange chromatography on DEAE-Sephacel and gel filtration on Sephacryl S-300. SDS-PAGE analysis ...
Structural studies of BmooMP alpha-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom
(Pergamon-Elsevier B.V. Ltd, 2010-02-01)
Hemostatically active snake venom metalloproteinases (SVMPs) perturb the blood coagulation cascade at specific points and due to their potential application as thrombolytic agents, the fibrin(ogen)olytic non-hemorrhagic ...
P-I metalloproteinases and L-amino acid oxidases from Bothrops species inhibit angiogenesis
(2021-01-01)
Background: Snake venoms are composed of pharmacologically active proteins that are evolutionarily diverse, stable and specific to targets. Hence, venoms have been explored as a source of bioactive molecules in treating ...
BJ-PI2, A non-hemorrhagic metalloproteinase from Bothrops jararaca snake venom
(Elsevier Science BvAmsterdamHolanda, 2012)
Batroxase, a new metalloproteinase from B. atrox snake venom with strong fibrinolytic activity
(PERGAMON-ELSEVIER SCIENCE LTDOXFORD, 2012)
The structures and functional activities of metalloproteinases from snake venoms have been widely studied because of the importance of these molecules in envenomation. Batroxase, which is a metalloproteinase isolated from ...