scholarly journals Biochemical, Pharmacological, and Structural Characterization of New Basic Bbil-TX fromBothriopsis bilineataSnake Venom

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Victor Corasolla Carregari ◽  
Rafael Stuani Floriano ◽  
Lea Rodrigues-Simioni ◽  
Flavia V. Winck ◽  
Paulo Aparecido Baldasso ◽  
...  
Keyword(s):  
Snake Venom ◽  
Protein Sequence ◽  
Maximal Activity ◽  
Optimal Conditions ◽  
High Identity ◽  
Phospholipid Hydrolysis ◽  
Rp Hplc ◽  
Crotalus Durissus ◽  
Didelphis Albiventris

Bbil-TX, a PLA2, was purified fromBothriopsis bilineatasnake venom after only one chromatographic step using RP-HPLC onμ-Bondapak C-18 column. A molecular mass of 14243.8 Da was confirmed by Q-Tof Ultima API ESI/MS (TOF MS mode) mass spectrometry. The partial protein sequence obtained was then submitted to BLASTp, with the search restricted to PLA2from snakes and shows high identity values when compared to other PLA2s. PLA2activity was presented in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 25–37∘C. Maximum PLA2activity required Ca2+and in the presence of Cd2+, Zn2+, Mn2+, and Mg2+it was reduced in the presence or absence of Ca2+. Crotapotin fromCrotalus durissus cascavellarattlesnake venom and antihemorrhagic factor DA2-II fromDidelphis albiventrisopossum sera under optimal conditions significantly inhibit the enzymatic activity. Bbil-TX induces myonecrosis in mice. The fraction does not show a significant cytotoxic activity in myotubes and myoblasts (C2C12). The inflammatory events induced in the serum of mice by Bbil-TX isolated fromBothriopsis bilineatasnake venom were investigated. An increase in vascular permeability and in the levels of TNF-a, IL-6, and IL-1 was was induced. Since Bbil-TX exerts a stronger proinflammatory effect, the phospholipid hydrolysis may be relevant for these phenomena.

Biochemical, Pharmacological and Structural Characterization of Two PLA2 Isoforms Cdr-12 and Cdr-13 from Crotalus durissus ruruima Snake Venom

2007 ◽  
Vol 26 (1) ◽  
pp. 39-49 ◽  
Author(s):  
Luis Alberto Ponce-Soto ◽  
Paulo Aparecido Baldasso ◽  
Frey Francisco Romero-Vargas ◽  
Flávia V. Winck ◽  
José Camillo Novello ◽  
...  
Keyword(s):  
Snake Venom ◽  
Structural Characterization ◽  
Crotalus Durissus

scholarly journals Unmasking Snake Venom ofBothrops leucurus: Purification and Pharmacological and Structural Characterization of New PL Bleu TX-III

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Fábio André Marangoni ◽  
Luis Alberto Ponce-Soto ◽  
Sergio Marangoni ◽  
Elen Cristina Teizem Landucci
Keyword(s):  
Snake Venom ◽  
Intravenous Route ◽  
Systemic Action ◽  
Phospholipid Hydrolysis ◽  
Multiple Alignments ◽  
Sds Page ◽  
One Step ◽  
High Degree

Bleu TX-III was isolated fromBothrops leucurussnake venom on one-step analytical chromatography reverse phase HPLC, was homogeneous on SDS-PAGE, and was confirmed by Q-Tof Ultima API ESI/MS (TOF MS mode) mass spectrometry in 14243.8 Da. Multiple alignments of Bleu TX-III show high degree of homology with basic PLA2myotoxins from otherBothropsvenoms. Our studies on local and systemic myotoxicity “in vivo” reveal that Bleu TX-III is myotoxin with local but not systemic action due to the decrease in the plasmatic CK levels when Bleu TX-III is administrated by intravenous route in mice (dose 1 and 5 μg). And at a dose of 20 μg myotoxin behaves like a local and systemic action. Bleu TX-III induced moderate marked paw edema, evidencing the local increase in vascular permeability. The inflammatory events induced in the mice (I.M.) were investigated. The increase in the levels of IL-1, IL-6, and TNF-αwas observed in the plasma. It is concluded that Bleu TX-III induces inflammatory events in this model. The enzymatic phospholipid hydrolysis may be relevant to these phenomena.Bothrops leucurusvenom is still not extensively explored, and the knowledge of its toxins separately through the study of structure/function will contribute for a better understanding of its action mechanism.

scholarly journals Biochemical Characterization and Pharmacological Properties of New Basic PLA2BrTX-I Isolated fromBothrops roedingeri(Roedinger's Lancehead) Mertens, 1942, Snake Venom

2013 ◽  
Vol 2013 ◽  
pp. 1-13 ◽  
Author(s):  
Mauricio Aurelio Gomes Heleno ◽  
Paulo Aparecido Baldasso ◽  
Luis Alberto Ponce-Soto ◽  
Sérgio Marangoni
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom ◽  
Biochemical Characterization ◽  
Maximal Activity ◽  
Total Amino Acid ◽  
Reverse Phase Hplc ◽  
Phospholipid Hydrolysis ◽  
High Amino Acid

BrTX-I, a PLA2, was purified fromBothrops roedingerivenom after only one chromatographic step using reverse-phase HPLC onμ-Bondapak C-18 column. A molecular mass of 14358.69 Da was determined by MALDI-TOF mass spectrometry. Amino acid analysis showed a high content of hydrophobic and basic amino acids as well as 14 half-cysteine residues. The total amino acid sequence was obtained using SwissProt database and showed high amino acid sequence identity with other PLA2from snake venom. The amino acid composition showed that BrTX-I has a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA2. BrTX-I presented PLA2activity and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0, 35–45°C, and required Ca2+.In vitro, the whole venom and BrTX-I caused a neuromuscular blockade in biventer cervicis preparations in a similar way to otherBothropsspecies. BrTX-I induced myonecrosis and oedema-forming activity analyzed through injection of the purified BrTX-I in mice. Since BrTX-I exerts a strong proinflammatory effect, the enzymatic phospholipid hydrolysis might be relevant for these phenomena; incrementing levels of IL-1, IL-6, and TNFαwere observed at 15 min, 30 min, one, two, and six hours postinjection, respectively.

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 Biological and Structural Characterization of Crotoxin and New Isoform of Crotoxin B PLA2 (F6a) from Crotalus durissus collilineatus Snake Venom

2007 ◽  
Vol 26 (4) ◽  
pp. 221-230 ◽  
Author(s):  
Luis Alberto Ponce-Soto ◽  
Bruno Lomonte ◽  
Lea Rodrigues-Simioni ◽  
José Camillo Novello ◽  
Sergio Marangoni
Keyword(s):  
Snake Venom ◽  
Structural Characterization ◽  
Crotalus Durissus ◽  
Crotalus Durissus Collilineatus

scholarly journals Bp-13 PLA2: Purification and Neuromuscular Activity of a New Asp49 Toxin Isolated fromBothrops pauloensisSnake Venom

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Georgina Sucasaca-Monzón ◽  
Priscila Randazzo-Moura ◽  
Thalita Rocha ◽  
Frank Denis Torres-Huaco ◽  
Augusto Vilca-Quispe ◽  
...  
Keyword(s):  
Contractile Response ◽  
Maximal Activity ◽  
Direct Electrical Stimulation ◽  
Terminal Sequence ◽  
Pharmacological Characterization ◽  
Neuromuscular Activity ◽  
Rp Hplc ◽  
Main Effect ◽  
High Degree

A new PLA2(Bp-13) was purified fromBothrops pauloensissnake venom after a single chromatographic step of RP-HPLC onμ-Bondapak C-18. Amino acid analysis showed a high content of hydrophobic and basic amino acids and 14 half-cysteine residues. The N-terminal sequence showed a high degree of homology with basic Asp49 PLA2myotoxins from otherBothropsvenoms. Bp-13 showed allosteric enzymatic behavior and maximal activity at pH 8.1, 36°–45°C. Full Bp-13 PLA2activity required Ca2+; its PLA2activity was inhibited by Mg2+, Mn2+, Sr2+, and Cd2+in the presence and absence of 1 mM Ca2+. In the mouse phrenic nerve-diaphragm (PND) preparation, the time for 50% paralysis was concentration-dependent (P<0.05). Both the replacement of Ca2+by Sr2+and temperature lowering (24°C) inhibited the Bp-13 PLA2-induced twitch-tension blockade. Bp-13 PLA2inhibited the contractile response to direct electrical stimulation in curarized mouse PND preparation corroborating its contracture effect. In biventer cervicis preparations, Bp-13 induced irreversible twitch-tension blockade and the KCl evoked contracture was partially, but significantly, inhibited (P>0.05). The main effect of this new Asp49 PLA2ofBothrops pauloensisvenom is on muscle fiber sarcolemma, with avian preparation being less responsive than rodent preparation. The study enhances biochemical and pharmacological characterization ofB. pauloensisvenom.

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