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| Elífio-Esposito,S. L.; Hess,P. L.; Moreno,A. N.; Lopes-Ferreira,M.; Ricart,C. A. O.; Souza,M. V.; Hasselman-Zielinski,F.; Becker,J. A.; Pereira,L. F.. |
| Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Venoms; Fibronectins; Vitronectin; Snakes; Intravital microscopy; Leukocytes. |
| Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009 |
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| Santos,LD; Pieroni,M; Menegasso,ARS; Pinto,JRAS; Palma,MS. |
| Venoms represent a huge and essentially unexplored reservoir of bioactive components that may cure diseases that do not respond to currently available therapies. This review select advances reported in the literature from 2000 to the present about the new scenario of Hymenoptera venom composition. On account of new technologies in the proteomic approach, which presents high resolution and sensitivity, the combination of developments in new instruments, fragmentation methods, strategic analysis, and mass spectrometry have become indispensable tools for interrogation of protein expression, molecule interaction, and post- translational modifications. Thus, the biochemical characterization of Hymenoptera venom has become a major subject of research in the area... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Hymenoptera; Venoms; Allergens; Phospholipase A1; Wasp venom antigen 5; Hyaluronoglucosaminidase; Mass spectrometry; Proteomics. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000400003 |
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| LIPPS,B. V.. |
| Lethal Toxin Neutralizing Factor (N-LTNF), MW 63.0 kDa, was isolated from opossum serum. After trypsin digestion, the active domain of N-LTNF was isolated and sequenced. The synthetic peptide consisting of ten amino acids was designated as LT-10. N-LTNF and LT-10 inhibited the lethality of animal, plant and bacteria toxins when tested on mice non-immunologically. The antibodies against N-LTNF and LT-10 only reacted immunologically with toxins and not with non-toxic substances. Anti-LTNF and anti-LT-10 reacted immunologically by ELISA test with toxins that were not detected by mouse test, such as cholera toxin and digoxin. Anti-LTNF and anti-LT-10 failed to react immunologically with non-toxic substances, such as nerve growth factor and collagen. Currently,... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Antibodies; In vitro assay; Lethal toxin neutralizing factor; Toxins; Venoms. |
| Ano: 2002 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302002000200003 |
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| Nekaris,K Anne-Isola; Moore,Richard S; Rode,E Johanna; Fry,Bryan G. |
| Only seven types of mammals are known to be venomous, including slow lorises (Nycticebus spp.). Despite the evolutionary significance of this unique adaptation amongst Nycticebus, the structure and function of slow loris venom is only just beginning to be understood. Here we review what is known about the chemical structure of slow loris venom. Research on a handful of captive samples from three of eight slow loris species reveals that the protein within slow loris venom resembles the disulphide-bridged heterodimeric structure of Fel-d1, more commonly known as cat allergen. In a comparison of N. pygmaeus and N. coucang, 212 and 68 compounds were found, respectively. Venom is activated by combining the oil from the brachial arm gland with saliva, and can... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Venoms; Ecology; Primates; Intraspecific competition; Predation; Ectoparasite; Naja naja. |
| Ano: 2013 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100203 |
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| Petretski,J.H.; Kanashiro,M.; Silva,C.P.; Alves,E.W.; Kipnis,T.L.. |
| This article describes the presence of two new forms of a thrombin-like enzyme, both with apparent molecular masses of 38 kDa, in Bothrops atrox venom. Both share the ability to cleave fibrinogen into fibrin and to digest casein. Both present identical Km on the substrate BApNA. Their N-terminal amino acid sequences are identical for 26 residues, sharing 80% homology with batroxobin and flavoxobin. Two groups of monoclonal antibodies (mAbs) raised against the purified enzyme forms recognized different epitopes of the putative corresponding enzymes present in B. atrox crude venom. On Western blotting analysis of B. atrox crude venom, mAbs 5DB2C8, 5AA10 and 5CF11, but not mAbs 6CC5 and 6AD2-G5, revealed two or more protein bands ranging from 25 to 38 kDa. By... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Venoms; Bothrops atrox; Enzymes; Thrombin-like enzymes; Blood coagulation system. |
| Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000001100005 |
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