Covalent structure and some pharmacological features of native and cleaved alpha-KTx12-1, a four disulfide-bridged toxin from Tityus serrulatus venom.
J Pept Sci
; 9(2): 132-40, 2003 Feb.
Article
em En
| MEDLINE
| ID: mdl-12630699
ABSTRACT
A toxin with four disulfide bridges from Tityus serrulatus venom was able to compete with 125I-kaliotoxin on rat brain synaptosomal preparations, with an IC50 of 46 nM. The obtained amino acid sequence and molecular mass are identical to the previously described butantoxin. Enzymatic cleavages in the native peptide followed by mass spectrometry peptide mapping analysis were used to determine the disulfide bridge pattern of alpha-KTx12-1. Also, after the cleavage of the first six N-terminal residues, including the unusual disulfide bridge which forms an N-terminus ring, the potency of the cleaved peptide was found to decrease about 100 fold compared with the native protein.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Venenos de Escorpião
/
Escorpiões
/
Dissulfetos
Limite:
Animals
Idioma:
En
Revista:
J Pept Sci
Ano de publicação:
2003
Tipo de documento:
Article