Please use this identifier to cite or link to this item: http://imsear.hellis.org/handle/123456789/150293
Title: Isolation, characterization and antigenic cross-reactivities of the major hemorrhagin from Cryptelytrops purpureomaculatus venom.
Authors: Fung, Shin Yee
Tan, Nget Hong
Keywords: Cryptelytrops purpureomaculatus
ELISA
Snake venom hemorrhagin
Taxonomy
Trimeresurus complex
Issue Date: Dec-2013
Citation: Fung Shin Yee, Tan Nget Hong. Isolation, characterization and antigenic cross-reactivities of the major hemorrhagin from Cryptelytrops purpureomaculatus venom. Indian Journal of Experimental Biology. 2013 Dec; 51(12): 1063-1069.
Abstract: The major hemorrhagin from C. purpureomaculatus (mangrove pit viper) venom was purified to homogeneity and termed Maculatoxin. Maculatoxin has a molecular weight of 38 kDa as determined by SDS-PAGE. It is an acidic protein (pI= 4.2) and exhibited proteolytic and hemorrhagic activities (MHD10 = 0.84 μg in mice) but was not lethal to mice at a dose of 1 μg/g. The hemorrhagic activity of Maculatoxin was completely inactivated by EDTA and partially inhibited by ATP and citrate. The N-terminal sequence of Maculatoxin (TPEQQRFPPTYIDLGIFVDHGMYAT) shares a significant degree of homology with the metalloprotease domain of other venom hemorrhagins. Indirect ELISA showed anti-Maculatoxin cross reacted with protein components of many snake venoms. In the double-sandwich ELISA, however, anti-Maculatoxin cross-reacted only with venoms of certain species of the Trimeresurus (Asia lance-head viper) complex, and the results support the recent proposed taxonomy changes concerning the Trimeresurus complex
URI: http://imsear.hellis.org/handle/123456789/150293
Appears in Collections:Indian Journal of Experimental Biology

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