Snake venom proteins are potential sources for novel drug design both for treatment of snake bites and for human genetic disorders. To achieve these, the basic sequence, structure and functional relationships of venom proteins should be understood. Proteolytic enzymes such as metallo and serine proteases are the major components of venom in vipers and are responsible for local and systematic envenomation effects. We have purified, partially sequenced and functionally characterised a serine protease, rhinocerase from the venom of Bitis gabonica rhinoceros. Rhinocerase is a multifunctional enzyme with kininogenase, clotting and defibrase activities.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:501321 |
| Date | January 2008 |
| Creators | Vaiyapuri, Sakthivel |
| Publisher | University of Reading |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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