scholarly journals A method for faster purification of serine proteinases from Bothrops alternatus and Bothrops moojeni snake venoms

2018 ◽  
Author(s):  
M.A.G. Heleno ◽  
L.D. Santos ◽  
R.S. Ferreira ◽  
B Barraviera
Keyword(s):  
Snake Venom ◽  
Fibrin Sealant ◽  
Biological Activities ◽  
Serine Proteinases ◽  
Snake Venoms ◽  
Bovine Thrombin ◽  
Bothrops Alternatus ◽  
Chromatographic Procedure ◽  
Crotalus Durissus ◽  
Bothrops Moojeni

ABSTRACTSnake venoms are important sources of substances with a variety of pharmacological activities. Among the different proteins present in these venoms, snake venom serine proteinases (SVSPs) have important effects on the hemostatic system that influence the hemodynamic properties of blood. Bothrops genus snakes presented their venom richly composed of SVSPs thrombin-like, and the isolation of these enzymes is of great interest. In 1994, the Center for the Study of Venoms and Venomous Animals (CEVAP) - UNESP standardized the fibrin sealant derived from snake venom, replacing the bovine thrombin by gyroxin thrombin-like enzyme from Crotalus durissus terrificus (Rattlesnake) and human plasma fibrinogen by buffaloes cryoprecipitate. Despite chromatographic techniques for the purification of gyroxin be well grounded in the literature, that income is considered low. Thus, in addition to gyroxin, other thrombin-like enzymes could be employed in the composition of the new fibrin sealant after being standardized to the purifying and chromatographic performance and widely evaluated for biological activities. Therefore, it is extremely important that in our lab is deployed, standardized and validated a method for the chromatographic purification of other thrombin-like enzymes such as found in Bothrops snake venoms. Thus a two-step chromatographic procedure was developed to routinely purify serine proteinases from Bothrops alternatus and B. moojeni snakes venoms to provide new enzymes for improving the CEVAP’s heterologous fibrin sealant.

Biochemical and biological characterization of two serine proteinases from Colombian Crotalus durissus cumanensis snake venom

Toxicon ◽  
2013 ◽  
Vol 63 ◽  
pp. 32-43 ◽  
Author(s):  
Arley Camilo Patiño ◽  
Jaime Andrés Pereañez ◽  
José María Gutiérrez ◽  
Alexandra Rucavado
Keyword(s):  
Snake Venom ◽  
Serine Proteinases ◽  
Biological Characterization ◽  
Crotalus Durissus ◽  
Crotalus Durissus Cumanensis

scholarly journals Rapid purification of serine proteinases from Bothrops alternatus and Bothrops moojeni venoms

Toxicon ◽  
2013 ◽  
Vol 76 ◽  
pp. 282-290 ◽  
Author(s):  
Liliane Maria Fernandes de Oliveira ◽  
Anwar Ullah ◽  
Rehana Masood ◽  
André Zelanis ◽  
Patrick J. Spencer ◽  
...  
Keyword(s):  
Serine Proteinases ◽  
Bothrops Alternatus ◽  
Rapid Purification ◽  
Bothrops Moojeni

scholarly journals Inhibitory Effect of PlantManilkara subsericeaagainst Biological Activities ofLachesis mutaSnake Venom

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Eduardo Coriolano De Oliveira ◽  
Caio Pinho Fernandes ◽  
Eladio Flores Sanchez ◽  
Leandro Rocha ◽  
André Lopes Fuly
Keyword(s):  
Ethyl Acetate ◽  
Snake Venom ◽  
Biological Activities ◽  
Inhibitory Effect ◽  
Snake Venoms ◽  
Brazilian Flora ◽  
Inhibitory Potential ◽  
Lachesis Muta

Snake venom is composed of a mixture of substances that caused in victims a variety of pathophysiological effects. Besides antivenom, literature has described plants able to inhibit injuries and lethal activities induced by snake venoms. This work describes the inhibitory potential of ethanol, hexane, ethyl acetate, or dichloromethane extracts and fractions from stem and leaves ofManilkara subsericeaagainstin vivo(hemorrhagic and edema) andin vitro(clotting, hemolysis, and proteolysis) activities caused byLachesis mutavenom. All the tested activities were totally or at least partially reduced byM. subsericea. However, whenL. mutavenom was injected into mice 15 min first or after the materials, hemorrhage and edema were not inhibited. Thus,M. subsericeacould be used as antivenom in snakebites ofL. muta. And, this work also highlights Brazilian flora as a rich source of molecules with antivenom properties.

scholarly journals Comparative analysis of local effects caused by Bothrops alternatus and Bothrops moojeni snake venoms: enzymatic contributions and inflammatory modulations

Toxicon ◽  
2016 ◽  
Vol 117 ◽  
pp. 37-45 ◽  
Author(s):  
Carla Cristine Neves Mamede ◽  
Bruna Barbosa de Sousa ◽  
Déborah Fernanda da Cunha Pereira ◽  
Mariana Santos Matias ◽  
Mayara Ribeiro de Queiroz ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Snake Venoms ◽  
Local Effects ◽  
Bothrops Alternatus ◽  
Bothrops Moojeni

scholarly journals Contribution of mast cells to the oedema induced by Bothrops moojeni snake venom and a pharmacological assessment of the inflammatory mediators involved

Toxicon ◽  
2010 ◽  
Vol 55 (2-3) ◽  
pp. 343-352 ◽  
Author(s):  
Neide Galvão Nascimento ◽  
Marlos Cortez Sampaio ◽  
Renata Amaral Olivo ◽  
Catarina Teixeira
Keyword(s):  
Mast Cells ◽  
Snake Venom ◽  
Inflammatory Mediators ◽  
Bothrops Moojeni

L-aminoacid oxidase from Crotalus durissus terrificus snake venom and its antibacterial potential

Toxicon ◽  
2019 ◽  
Vol 168 ◽  
pp. S13
Author(s):  
Leonardo Melo ◽  
Lidiane Nunes Barbosa ◽  
Rui Seabra Ferreira Junior ◽  
Benedito Barraviera ◽  
Luciana Curtolo De Barros ◽  
...  
Keyword(s):  
Snake Venom ◽  
Crotalus Durissus Terrificus ◽  
Crotalus Durissus ◽  
Antibacterial Potential

scholarly journals Caryospora bigenetica (Apicomplexa: Eimeriidae) in South America: new hosts and distribution records

2015 ◽  
Vol 24 (1) ◽  
pp. 101-104 ◽  
Author(s):  
Lúcio André Viana ◽  
Kamilla Costa Mecchi ◽  
Leonardo França do Nascimento ◽  
Heitor Miraglia Herrera ◽  
Paula Helena Santa-Rita ◽  
...  
Keyword(s):  
South America ◽  
Polar Granule ◽  
First Record ◽  
Stieda Body ◽  
Mato Grosso ◽  
Sporocyst Residuum ◽  
The Family ◽  
New Hosts ◽  
Crotalus Durissus ◽  
Bothrops Moojeni

The coccidian Caryospora bigenetica was first described in the snake Crotalus horridus (Viperidae) from United States of America. This study represents the first record of the occurrence of C. bigenetica in snakes in South America. Feces were sampled between November 2013 and May 2014 from 256 wild snakes maintained in scientific breeding facilities in the states of Mato Grosso do Sul (MS; n = 214) and Rio de Janeiro (RJ; n = 42), Brazil. Caryospora bigenetica was found in 14 (5.6%) snakes, all belonging to the family Viperidae. Ten Bothrops moojeni and two Crotalus durissus from MS were infected. The coccidian was also found in one C. durissus and in one Bothrops jararacussu from the state of RJ. The oocysts were spherical with a double wall, the exterior lightly mammillated, striations apparent in transverse view, 13.0 µm (12 – 14); polar granule fixed in the internal wall. Sporocysts oval or pyriform, 10.0 × 8.0 µm (9 – 11 × 8 – 9); Stieda body discoid; sub-Stieda body present; sporocyst residuum present, formed by a group of spheroid bodies between sporozoites. This study increases the number of viperid hosts of C. bigenetica and expands the geographical distribution to South America.

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