Portal de Periódicos da CAPES

Process Development for Antibody Purification from Tobacco by Protein A Affinity Chromatography

2011; Wiley; Volume: 35; Issue: 1 Linguagem: Inglês

10.1002/ceat.201100259

1521-4125

Carolyn McKenzie Hey, C. Zhang,

Toxin Mechanisms and Immunotoxins

Abstract Tobacco is possibly the most promising plant for plant‐made pharmaceuticals, e.g., antibodies, due to its high biomass yields and robust transformation technology. Protein A affinity chromatography is commonly used for antibody purification, however, direct application of tobacco extract to protein A chromatography columns may be problematic due to the nonspecific binding of native tobacco proteins (NTPs). Three different protein A resins, ProSep‐vA High Capacity, Ultra, and Ultra Plus, from Millipore were studied for antibody purification from tobacco. Experiments were run with extracts from nontransgenic tobacco and the model antibody, human immunoglobulin G (IgG). The efficiency of the wash buffers to reduce nonspecific binding of NTPs to the resins was evaluated by altering the ionic strength and pH. Considering all factors, Ultra Plus Protein A resin may be the best in antibody purification from tobacco.