Related Experiment Video
Updated: Jul 5, 2026
Extraction of Venom and Venom Gland Microdissections from Spiders for Proteomic and Transcriptomic Analyses
Published on: November 3, 2014
Purification and complete primary structure of the first PLA2 from Lachesis stenophrys (the Central American
Eduardo Borges de Assis1, Maria Inácia Estevão-Costa, Ana do Carmo Valentim
1Laboratory of Molecular and Cell Biology, Division of Biomedical Sciences, Fundação Ezequiel Dias, Rua Conde Pereira Carneiro 80, CEP 30510-010, Belo Horizonte, MG, Brazil.
Abstract:
The first PLA(2) (LsPA-1) from L. stenophrys snake venom was purified to homogeneity using three chromatographic steps and had its complete primary structure determined. An average molecular mass of 13,870.3 kDa was determined by mass spectrometry and a 3.3-fold increase in the PLA(2) activity was observed for LsPA-1 as compared to the whole venom. Multiple alignment of PLA(2) from Lachesis spp. snakes suggested the existence of two geographical clades for this genus in the New World, which is in accordance with morphological, behavioral and mtDNA data obtained by others. Phospholipases A(2) from Crotalus spp. snake venoms were similarly distributed into two groups. Intergroup analysis indicated that most amino acid substitutions were observed in the amino- and carboxy-terminal regions of the molecules in each clade. Both regions have been suggested to play important roles in determining the biological properties of PLA(2) from snake venoms. The dendogram derived for PLA(2) from Lachesis and Crotalus snakes highlighted the phylogenetic relationships between these two genera in the New World.
