Use of commercial anion-exchange resins as solid support for peptide synthesis and affinity chromatography

Nenhuma Miniatura disponível

Data

2003-07-01

Orientador

Coorientador

Pós-graduação

Curso de graduação

Título da Revista

ISSN da Revista

Título de Volume

Editor

Elsevier B.V.

Tipo

Artigo

Direito de acesso

Acesso restrito

Resumo

This report demonstrates that due to the presence of residual reactive sites in their matrices, classical diethylaminoethyl-attaching commercial anion-exchanger resins such as DEAE-MacroPrep and DEAE-Sephadex A50 supports can be used for peptide synthesis. Moreover, due to the high stability of the peptide-resin bond in the final cleavage treatments, desired peptidyl-resins free of side-chain protecting groups, which enables them to be further used as solid support for affinity chromatography, can be obtained. To demonstrate this potentiality, a fragment corresponding to the antigenic and immunodominant epitope of sporozoites of the Plasmodium falciparum malaria parasite was synthesized in these traditional resins and antibody molecules generated against the peptide sequence were successfully retained in these peptidyl supports. Due to the maintenance of their original anion-exchange capacities, the present findings open the unique possibility of applying, simultaneously, dual anion-exchange and affinity procedures for purification of a variety of macromolecules. (C) 2003 Elsevier B.V. (USA). All rights reserved.

Descrição

Idioma

Inglês

Como citar

Analytical Biochemistry. San Diego: Academic Press Inc. Elsevier B.V., v. 318, n. 1, p. 39-46, 2003.

Itens relacionados

Financiadores