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Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
(2008-01)
A serine proteinase with thrombin-like activity was isolated from the venom of the Central American pit viper Bothrops asper. Isolation was performed by a combination of affinity chromatography on aminobenzamidine-Sepharose ...
Membrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinases
(2004-12-01)
ProMMP-2 activation by Bothrops asper venom was investigated in mouse gastrocnemius muscle, mammalian cell culture and a cell-free system. Zymography revealed an increment of latent and activated forms of MMP-2 in muscle ...
Biochemical and biological characterization of two serine proteinases from Colombian Crotalus durissus cumanensis snake venom
(2013-03-01)
Two clotting serine proteinases, named Cdc SI and Cdc SII, were isolated and characterized for the first time from Colombian Crotalus durissus cumanensis snake venom. The enzymes were purified using two chromatographic ...
Characterization of a novel snake venom component: Kazal-type inhibitor-like protein from the arboreal pitviper Bothriechis schlegelii
(2016-06)
Snake venoms are composed mainly of a mixture of proteins and peptides. Notably, all snake venom toxins have been assigned to a small number of protein families. Proteomic studies on snake venoms have recently identified ...
Novel catalytically-inactive PII metalloproteinases from a viperid snake venom with substitutions in the canonical zinc-binding motif
(2016-10-12)
Snake venom metalloproteinases (SVMPs) play key biological roles in prey immobilization
and digestion. The majority of these activities depend on the hydrolysis of relevant protein substrates
in the tissues. Hereby, we ...
Local and systemic pathophysiological alterations induced by a serine proteinase from the venom of the snake Bothrops jararacussu
(2007-06-01)
The local and systemic pathophysiological alterations induced by BjussuSP-I, a thrombin-like serine proteinase from the venom of the snake Bothrops jararacussu, were assessed in mice. BjussuSP-I induced a mild edema but ...
Extracts of Renealmia alpinia (Rottb.) MAAS Protect against Lethality and Systemic Hemorrhage Induced by Bothrops asper Venom: Insights from a Model with Extract Administration before Venom Injection
(2015)
Renealmia alpinia (Rottb.) MAAS, obtained by micropropagation (in vitro) and
wild forms have previously been shown to inhibit some toxic activities of Bothrops asper
snake venom if preincubated before injection. In this ...
High resolution analysis of snake venom metalloproteinase (SVMP) peptide bond cleavage specificity using proteome based peptide libraries and mass spectrometry
(2011-04-01)
Both serine and metalloproteinases have been shown to play the role of toxins in the venoms of many snakes. Determination of the natural protein substrates of these toxins is an important feature in the toxinological ...
Thrombocytopenia and platelet hypoaggregation induced by Bothrops asper snake venom. Toxins involved and their contribution to metalloproteinase-induced pulmonary hemorrhage.
(2005-07)
Thrombocytopenia and platelet dysfunction occur in patients bitten by Bothrops sp snakes in Latin America. An experimental model was developed in mice to study the effects of B. asper venom in platelet numbers and function. ...
Antivenomics of Atropoides mexicanus and Atropoides picadoi snake venoms: Relationship to the neutralization of toxic and enzymatic activities
(2010-09-30)
Viperid snakes of the genus Atropoides are distributed in Mexico and Central America and, owing to their size and venom yield, are capable of provoking severe envenomings in humans. This study evaluated, using an ‘antivenomics’ ...