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

被引：8

作者：

de Assis, Eduardo Borges ^{[2
]}

Estevao-Costa, Maria Inacia ^{[2
]}

Valentim, Ana do Carmo ^{[2
]}

Silva-Neto, Aristeu ^{[2
]}

Cotta, Giselle Agostini ^{[3
]}

Mudado, Mauricio Alvarenga ^{[2
]}

Richardson, Michael ^{[2
]}

Fortes-Dias, Consuelo Latorre ^{[1
]}

机构：

[1] Fundacao Ezequiel Dias DPD, BR-30510010 Belo Horizonte, MG, Brazil

[2] Fundacao Ezequiel Dias FUNED, Div Biomed Sci, Lab Mol & Cell Biol, BR-30510010 Belo Horizonte, MG, Brazil

[3] Fundacao Ezequiel Dias FUNED, Div Immunobiol, BR-30510010 Belo Horizonte, MG, Brazil

来源：

PROTEIN JOURNAL | 2008年 / 27卷 / 05期

关键词：

phospholipase A(2); Lachesis stenophrys; Lachesis; Viperidae; snake venom;

D O I：

10.1007/s10930-008-9141-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：327 / 333

页数：7