Sequence, structure and functional studies of viper venom proteolytic enzymes

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 prot...

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Main Author: Vaiyapuri, Sakthivel
Published: University of Reading 2008
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Online Access:http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.501321
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spelling ndltd-bl.uk-oai-ethos.bl.uk-5013212016-06-21T03:32:06ZSequence, structure and functional studies of viper venom proteolytic enzymesVaiyapuri, Sakthivel2008Snake 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.615.942University of Readinghttp://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.501321Electronic Thesis or Dissertation
collection NDLTD
sources NDLTD
topic 615.942
spellingShingle 615.942
Vaiyapuri, Sakthivel
Sequence, structure and functional studies of viper venom proteolytic enzymes
description 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.
author Vaiyapuri, Sakthivel
author_facet Vaiyapuri, Sakthivel
author_sort Vaiyapuri, Sakthivel
title Sequence, structure and functional studies of viper venom proteolytic enzymes
title_short Sequence, structure and functional studies of viper venom proteolytic enzymes
title_full Sequence, structure and functional studies of viper venom proteolytic enzymes
title_fullStr Sequence, structure and functional studies of viper venom proteolytic enzymes
title_full_unstemmed Sequence, structure and functional studies of viper venom proteolytic enzymes
title_sort sequence, structure and functional studies of viper venom proteolytic enzymes
publisher University of Reading
publishDate 2008
url http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.501321
work_keys_str_mv AT vaiyapurisakthivel sequencestructureandfunctionalstudiesofvipervenomproteolyticenzymes
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