Document Type
Article
Publication Date
8-2011
Abstract
Serine proteases are widely found in snake venoms. They have variety of functions including contributions to hemostasis. In this study, five serine proteases were cloned and characterized from two different cDNA libraries: factor V activator (RVV-V), alpha fibrinogenase (RVAF) and beta fibrinogenase (RVBF) from Russell's viper (Daboia russelli siamensis), and plasminogen activator (APL-PA) and protein C activator (APL-C) from Agkistrodon piscivorus leucostoma. The snake venom serine proteases were clustered in phylogenetic tree according to their functions. KA/KS values suggested that accelerated evolution has occurred in the mature protein coding regions in cDNAs of snake venom serine proteases.
Recommended Citation
Sukkapan, P., Jia, Y., Nuchprayoon, I., & Pérez, J. C. (2011). Phylogenetic analysis of serine proteases from Russell's viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom. Toxicon : official journal of the International Society on Toxinology, 58(2), 168–178. https://doi.org/10.1016/j.toxicon.2011.05.014
Publication Title
Toxicon
DOI
10.1016/j.toxicon.2011.05.014
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