Monoclonal antibody purification by affinity chromatography with ligands derived from the screening of peptide combinatory libraries

被引：0

作者：

S.A. Camperi

N.B. Iannucci

G.J. Albanesi

M. Oggero Eberhardt

M. Etcheverrigaray

A. Messeguer

F. Albericio

O. Cascone

机构：

[1] Universidad de Buenos Aires,Cátedra de Microbiología Industrial y Biotecnología, Facultad de Farmacia y Bioquímica

[2] Universidad Nacional del Litoral,Laboratorio de Cultivos Celulares, Facultad de Bioquímica y Ciencias Biológicas

[3] Instituto de Investigaciones Bioquímicas y Ambientales (CSIC),Departamento de Química Orgánica, Facultad de Química

[4] Universidad de Barcelona,undefined

来源：

Biotechnology Letters | 2003年 / 25卷

关键词：

affinity chromatography; combinatorial library; monoclonal antibody purification; peptide ligands;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

The peptide, Ala-Pro-Ala-Arg (APAR), was selected from the screening of a tetrapeptide combinatorial synthetic library as the ligand for affinity purification of an anti-Granulocyte Macrophage-Colony Stimulating Factor (GM-CSF) monoclonal antibody (Mab) developed in mouse ascitis. The affinity chromatographic matrix obtained by attachment of APAR to agarose, having a peptide density of 0.5 μmol ml−1, showed a maximum capacity of 9.1 mg Mab ml−1 and a dynamic capacity of 3.9 mg Mab ml−1. A 95% yield of electrophoretically pure anti-GM-CSF was obtained in a single step.

引用

页码：1545 / 1548

页数：3

共 26 条

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