| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1217231 | Journal of Chromatography B | 2007 | 12 Pages |
Abstract
A basic toxin from Russell's viper venom of 7.2 kDa (RVV-7) has been purified to homogeneity after partial unfolding by 4 M urea followed by filtration through Centricon-30 membrane. Its N-terminal sequence showed strong homology with snake venom cytotoxins. Cytotoxic activity of RVV-7 has been demonstrated with B16F10 melanoma cells. PLA2 activity was observed in cytotoxin (CX3) from Naja kauthia bearing sequence homology with RVV-7. Phospholipase A2 and trypsin inhibitory activities were also observed with RVV-7. Chemical modification and inhibition studies suggested independent functional sites for these activities. A qualitative assessment of tumor growth inhibition by RVV-7 has been made.
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Authors
Gargi Maity, Somnath Mandal, Amitabha Chatterjee, Debasish Bhattacharyya,