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Assessment of biomedical and pharmacological activities of sea anemones Stichodactyla mertensii and Stichodactyla gigantea from Gulf of Mannar Biosphere Reserve, southeast coast of India J. Venom. Anim. Toxins incl. Trop. Dis.
Thangaraj,S; Bragadeeswaran,S.
Cnidarians comprise an old and diverse animal phylum, and possess a wide variety of biologically active substances. Sea anemones contain a diversity of interesting biologically active compounds including some potent toxins. In the present work, the sea anemones Stichodactyla mertensii and Stichodactyla gigantea, collected from the Mandapam coast, are characterized biomedically and pharmacologically. The crude protein was obtained by using methanol and aqueous extracts. The respective protein contents of S. mertensii and S. gigantea were found to be 2.10 µg/mL and 1.87 µg/mL. The methanol and aqueous extracts of S. mertensii and S. gigantea yielded six and nine bands by SDS-PAGE on 12% gel. In the hemolytic assay, both extracts exhibited hemolytic effect on...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Aqueous extract; Neurotoxicity; Mouse bioassay; Analgesic activity.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000100007
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Proteomic characterization of the thermostable toxins from Naja naja venom J. Venom. Anim. Toxins incl. Trop. Dis.
Binh,DV; Thanh,TT; Chi,PV.
Naja naja snake venom presents abundant thermostable peptides. Many of them possess useful pharmacological activity that may be employed for drug development. For the proteomic characterization of such toxins, in the present study, Naja naja venom solution was heated up to 100°C for 10, 30, 60, 120, 180 and 300 minutes and protein fractions of non-heated and heated venom were analyzed by two-dimensional nano-liquid chromatography coupled online with tandem mass spectrometry. After heating for 300 minutes, a total of 32 peptides were still detected in the supernatant. The identified peptides belong to the following groups: cardiotoxins, neurotoxins and cytotoxins. It was found that thermostable peptides are able to preserve their analgesic activity after a...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Naja naja; Snake venom proteome; Thermostable peptides; Mass spectrometry; Analgesic activity.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000400014
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