RESUMO
Two phospholipases were found in the venom of Bungarus fasciatus, one in fraction III, the other in fraction X of the chromatographic separation. A neutral PLA2(III) purified from fraction III was subjected to amino acid sequencing by means of an automated sequenator applied to the intact RCM-PLA2 (III) and the individual peptides obtained from HPLC separation of the three types of enzymatic peptides. PLA(III) was shown to consist of 118 amino acid residues with 14 half-cystines. It is 65% homologous to the basic PLA2 obtained from fraction X.
Assuntos
Venenos Elapídicos/análise , Fosfolipases A/análise , Fosfolipases/análise , Venenos de Serpentes , Sequência de Aminoácidos , Animais , Cromatografia Líquida de Alta Pressão , Fosfolipases A2 do Grupo II , Dados de Sequência Molecular , Fosfolipases A2 , Proteínas de RépteisRESUMO
A basic phospholipase A2 (PLA2) was isolated and purified from the venom of Bungarus fasciatus. Four kinds of enzymes, lysyl endopeptidase, endoproteinase Asp-N, endoproteinase Glu-C and trypsin, were employed to elucidate the complete primary structure by means of gas-phase sequencing. The amino-acid sequence reveals 118 amino-acid residues containing seven pairs of half-cystine. It has 78% and 61% structural identities with PLA2 from Bungarus multicinctus and Naja melanoleuca DE-II, respectively.
