Hemorrhagic And Proteolytic Activity
Mostrando 1-12 de 15 artigos, teses e dissertações.
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1. Anti-ophidian activity of Bredemeyera floribunda Willd. (Polygalaceae) root extract on the local effects induced by Bothrops jararacussu venom
Bredemeyera floribunda roots are popularly used to treat snakebites in the semiarid region of Northeast Brazil, and previous studies indicate the anti-ophidian actions of triterpenoid saponins found in its roots. To assess B. floribunda root extract (BFRE) activity against the effects of Bothrops jararacussu venom (BjuV), antiphospholipasic, antiproteolytic,
Braz J Med Biol Res. Publicado em: 03/12/2018
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2. Pharmacological characterization of cnidarian extracts from the Caribbean Sea: evaluation of anti-snake venom and antitumor properties
Abstract Background: Cnidarians produce toxins, which are composed of different polypeptides that induce pharmacological effects of biotechnological interest, such as antitumor, antiophidic and anti-clotting activities. This study aimed to evaluate toxicological activities and potential as antitumor and antiophidic agents contained in total extracts from fi
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 21/09/2018
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3. The red seaweed Plocamium brasiliense shows anti-snake venom toxic effects
Background Snakebite is considered a neglected tropical disease by the World Health Organization. In Brazil, about 70% of the envenomation cases are caused by Bothrops snakes. Its venom may provoke hemorrhage, pain, necrosis, hemolysis, renal or cardiac failure and even death in victims. Since commercial antivenom does not efficiently neutralize the local t
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 03/03/2015
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4. Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography
Hypnale hypnale (hump-nosed pit viper) has been recently identified as one of the medically important venomous snakes in Sri Lanka and on the southwestern coast of India. The characterization of its venom is essential for understanding the pathophysiology of envenomation and for optimizing its management. In the present study, the biological properties of Hy
Journal of Venomous Animals and Toxins including Tropical Diseases. Publicado em: 2011
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5. Purification and functional characterization of a new non-hemorrhagic metalloprotease from Bothrops moojeni snake venom / Purificação e caracterização bioquímica da moozincina, uma metaloprotease dependente de zinco presente na peçonha da serpente Bothrops moojeni (Caiçaca)
Bothrops snake venoms contain proteases that contribute to the local effects seen after envenoming. In this study, a non-hemorrhagic metalloprotease was isolated from the venom of B. moojeni. The enzyme was isolated by a combination of ion exchange and gel filtration chromatographies and named Moozincin. The enzyme was purified to homogeneity as judged by it
Publicado em: 2010
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6. Purificação e caracterização bioquímica de BthMP: uma nova metaloprotenaise do veneno de Botrops moojeni (Caiçaca)
In this work a new metalloproteinase (BthMP) was purified from the snake venom of Bothrops moojeni. This enzyme was homogeneous by native and SDSPAGE it showed polypeptide chain of 23,5 kDa, pI = 7,1 and N-terminal blocked. BthMP is comprised of high proteolytic activity on casein, fibrin and bovine fibrinogen, but no coagulating, esterase, phospholipase A2
Publicado em: 2006
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7. Efeito da rACLF, uma metalopeptidase recombinante da peçonha de Agkistrodon contortrix laticinctus, na viabilidade celular, expressão de citocinas e degradação de proteínas da matriz extracelular.
ACLF is a fibrinolytic non-hemorrhagic metallopeptidase from the venom of the snake Agkistrodon contortrix laticinctus. rACLF is synthesized as a zymogen (pro- ACLF) with 412 aminoacids, while the active form of enzyme has 222 aminoacids. The ORF (open reading frame) that codes for the peptidase was isolated (from a cDNA venom gland library of A. contortrix.
Publicado em: 2006
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8. Caracterização funcional e estrutural de uma metaloprotease hemorrágica isolada da peçonha de Bothrops jararacussu. / Functional and structural characterization of a hemorrhagic metalloprotease isolated from Bothrops jararacussu snake venom
In this study the isolation, functional and structural characterization of a hemorrhagic metalloprotease, named BjussuMP-I is reported. The protein was isolated from Bothrops jararacussu snake venom by a combination of two chromatographic steps, using gel filtration on Sephacryl S-200 (0.01 M Tris-HCl, pH7.6 buffer) and Phenyl-Sepharose CL-4B chromatography
Publicado em: 2005
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9. Subclonagem e expressão do domínio catalítico da jararagina: estudo do efeito das modificações pós-traducionais na atividade hemorrágica.
Metalloproteases are Zn++-dependent peptidase enzymes, richly found in Crotalidae and Viperidae snake venoms. Most snake venom metalloproteases (svMPs) are active on extracellular matrix components and this effect is thought to result in bleeding as a consequence of the basement membrane disruption in capillaries. Jararhagin is a hemorrhagic svMP from Bothro
Publicado em: 2004
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10. Age-related biological activity of South American rattlesnake (Crotalus durissus terrificus) venom
An in vitro and in vivo comparative study was performed on the effects of Crotalus durissus terrificus venoms from a mother and its 15 newborns. The venoms were tested for protein content, lethality, proteolytic, myotoxic, hemorrhagic, and phospholipase A2 activity. The minimum coagulant dose in plasma and human fibrinogen, protrhombin, and Factor II activat
Journal of Venomous Animals and Toxins including Tropical Diseases. Publicado em: 2003
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11. Micrurus spixii (PERUVIAN CORAL SNAKE) VENOM - PRELIMINARY BIOCHEMICAL AND ENZYMATIC CHARACTERIZATION
Micrurus spixii venom was studied after fractionation by Sephadex G-100 SF gel filtration chromatography. Several enzymatic activities and biological effects were investigated in whole venom and fractions. The venom was resolved in four peaks in a range of about 73.2-10.7 kDa molecular weight. Alkaline phosphatase and acetylcholinesterase activities were fou
Journal of Venomous Animals and Toxins. Publicado em: 2002
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12. Characterization of the Hemorrhagic Reaction Caused by Vibrio vulnificus Metalloprotease, a Member of the Thermolysin Family
Vibrio vulnificus is an opportunistic human pathogen causing wound infections and septicemia, characterized by hemorrhagic and edematous damage to the skin. This human pathogen secretes a metalloprotease (V. vulnificus protease [VVP]) as an important virulence determinant. When several bacterial metalloproteases including VVP were injected intradermally into
American Society for Microbiology.