Hindered diffusion of proteins in mixture adsorption on porous anion exchangers and impact on flow-through purification of large proteins.

Complex adsorption kinetics behaviors of proteins in mixtures hampers chromatographic process development and complicates model-based prediction of separation. We investigated the adsorption characteristics of mixtures comprised of a larger protein (secretory immunoglobulins or thyroglobulin) and a smaller protein (serum albumin or green fluorescence protein) on the small-pore anion exchanger Q Sepharose FF. Confocal laser scanning microscopy measurements revealed that binding of the large protein was extremely slow and eventually stopped completely after the adsorption front penetrated just a few μm into the particle.

Secretory immunoglobulin purification from whey by chromatographic techniques.

Secretory immunoglobulins (SIg) are a major fraction of the mucosal immune system and represent potential drug candidates. So far, platform technologies for their purification do not exist. SIg from animal whey was used as a model to develop a simple, efficient and potentially generic chromatographic purification process.

A nonchromatographic process for purification of secretory immunoglobulins from caprine whey.

Secretory immunoglobulins are an important antibody class being primarily responsible for immunoprotection of mucosal surfaces. A simple, non-chromatographic purification process for secretory immunoglobulins from caprine whey was developed. In the first process step whey was concentrated 30-40-fold on a 500 kDa membrane, thereby increasing the purity from 3% to 15%.