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| Tan,NH; Fung,SY; Ponnudurai,G. |
| Bungarus flaviceps (red-headed krait) venom presents an intravenous LD50 of 0.32 μg/g and exhibits enzymatic activities similar to other Bungarus toxins. ELISA cross-reactions between anti-Bungarus flaviceps and a variety of elapid and viperid venoms were observed in the current study. Double-sandwich ELISA was highly specific, since anti-B. flaviceps serum did not cross-react with any tested venom, indicating that this assay can be used for species diagnosis in B. flaviceps bites. In the indirect ELISA, anti-B. flaviceps serum cross-reacted moderately with three different Bungarus venoms (9-18%) and Notechis scutatus venom, but minimally with other elapid and viperid toxins. The results indicated that B. flaviceps venom shares common epitopes with other... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bungarus flaviceps venom; Enzymes; ELISA; Neutralization. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000100014 |
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| Vejayan,J; Shin Yee,L; Ponnudurai,G; Ambu,S; Ibrahim,I. |
| Snake venoms comprise a highly complex mixture of proteins, which requires for their characterization the use of versatile two-dimensional electrophoresis techniques. In the present study, venoms obtained from eight snakes (Ophiophagus hannah, Naja kaouthia, Naja sumatrana, Bungarus fasciatus, Trimeresurus sumatranus, Tropidolaemus wagleri, Enhydrina schistosa and Calloselasma rhodostoma) commonly found in Malaysia were separated based on two independent properties, isoelectric point (pI) and molecular weight (MW). Many differences in snake venoms at the inter-family, inter-subfamily, inter-genus and inter-species levels were revealed. Notably, proteins from individuals of the Viperidae family - Trimeresurus sumatranus, Tropidolaemus wagleri and... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venom; Protein profile analysis; Two-dimensional gel electrophoresis; SDS-PAGE. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000400013 |
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| Phua,CS; Vejayan,J; Ambu,S; Ponnudurai,G; Gorajana,A. |
| Some constituents of snake venom have been found to display a variety of biological activities. The antibacterial property of snake venom, in particular, has gathered increasing scientific interest due to antibiotic resistance. In the present study, king cobra venom was screened against three strains of Staphylococcus aureus [including methicillin-resistant Staphylococcus aureus (MRSA)], three other species of gram-positive bacteria and six gram-negative bacteria. King cobra venom was active against all the 12 bacteria tested, and was most effective against Staphylococcus spp. (S. aureus and S. epidermidis). Subsequently, an antibacterial protein from king cobra venom was purified by gel filtration, anion exchange and heparin chromatography. Mass... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: L-amino acid oxidase; King cobra; Antibacterial activity; Ophiophagus hannah. |
| Ano: 2012 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000200010 |
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| Tan,CH; Sim,SM; Gnanathasan,CA; Fung,SY; Ponnudurai,G; Pailoor,J; Tan,NH. |
| 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 Hypnale hypnale venom and venom fractions obtained using Resource Q ion exchange chromatography were determined. The venom exhibited toxic activities typical of pit viper venom, comparable to that of its sister taxon, the Malayan pit viper (Calloselasma rhodostoma). Particularly noteworthy were its high activities of thrombin-like enzyme, proteases, phospholipase A2, L-amino acid oxidase and... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Hypnale hypnale; Venom; Enzymes; Toxins; Fibrinogen; Nephrotoxicity. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000400015 |
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