Please use this identifier to cite or link to this item:
Title: Use of commercial anion-exchange resins as solid support for peptide synthesis and affinity chromatography
Authors: Nakaie, C. R.
Lanzer, D. A.
Malavolta, L.
Cilli, E. M.
Rodrigues, M. M.
Universidade Federal de São Paulo (UNIFESP)
Univ Estadual Paulista
Keywords: peptide
ion-exchange chromatography
affinity chromatography
Issue Date: 1-Jul-2003
Publisher: Elsevier B.V.
Citation: Analytical Biochemistry. San Diego: Academic Press Inc Elsevier Science, v. 318, n. 1, p. 39-46, 2003.
Abstract: 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 Science (USA). All rights reserved.
ISSN: 0003-2697
Other Identifiers:
Appears in Collections:Em verificação - Geral

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.