Purification and complete primary structure of the first PLA2 from Lachesis stenophrys (the Central American Bushmaster) snake venom.
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.
de Assis
Eduardo Borges
EB
Laboratory of Molecular and Cell Biology, Division of Biomedical Sciences, Fundação Ezequiel Dias, Rua Conde Pereira Carneiro 80, CEP 30510-010, Belo Horizonte, MG, Brazil.
Estevão-Costa
Maria Inácia
MI
do Carmo Valentim
Ana
A
Silva-Neto
Aristeu
A
Agostini Cotta
Giselle
G
Alvarenga Mudado
Maurício
M
Richardson
Michael
M
Fortes-Dias
Consuelo Latorre
CL
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D017124:Conserved Sequence; D008969:Molecular Sequence Data; D054467:Phospholipases A2 / Q000737:chemistry* / Q000302:isolation & purification*; D010802:Phylogeny; D016415:Sequence Alignment; D012910:Snake Venoms / Q000201:enzymology* / Q000302:isolation & purification; D017819:Viperidae
D012910:Snake Venoms; D054467:Phospholipases A2