Purification and complete primary structure of the first PLA2 from Lachesis stenophrys (the Central American Bushmaster) snake venom.

摘要: The first PLA2 (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 determined by spectrometry a 3.3-fold increase in the activity observed for LsPA-1 as compared whole venom. Multiple alignment Lachesis spp. snakes suggested existence two geographical clades this genus New World, which is accordance with morphological, behavioral mtDNA data obtained others. Phospholipases A2 Crotalus venoms were similarly distributed into groups. Intergroup analysis indicated that most amino acid substitutions amino- carboxy-terminal regions molecules each clade. Both have been play important roles determining biological properties venoms. dendogram derived highlighted phylogenetic relationships between these genera World.