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Affinity Depletion Cartridges for Removal of Human Serum Albumin and Immunoglobulins from Human Serum

e stain. 2-D gel analysis was performed using 200 ug human serum, before and after affinity depletion by both cartridges and the proteins visualized by silver stain. MALDI-TOF peptide mass fingerprinting (PMF) was performed on bands from 1D Gel that did not correspond to the intact molecular weight of human Albumin using Voyager DE STR Biospectrometry Workstation (ABI) from in-gel digested peptides using 10ug/mL modified bovine trypsin in 25mM ammonium bicarbonate.

Anti-HSA and anti-human IgG ELISA kits (Bethyl Laboratory) were run according to the manufacture protocol. The flow-through fractions used for the ELISA were pooled from multiple runs (six runs from two Anti-HSA cartridges from the same lot and four runs from two Protein G cartridges from the same lot).

Results and Discussion:

Figure 1 shows the chromatograph of affinity depletion of HSA from human serum using the POROS Anti-HSA antibody affinity cartridge operated on the Vision Workstation. The sample was previously run over a POROS protein G cartridge in order to remove IgG from the solution. The separations can be performed separately or in tandem in minutes using an auto-mated Multidimensional Workstation such as the VISION Workstation as well as being performed manually using a syringe inlet adapter.

Figure 2 shows SDS-PAGE analysis of serum sample (lane2) the flowthrough and eluted fractions and the enrichment of low intensity bands in the protein G and Anti-HSA FT fraction (lane 5). The predominant proteins in the eluted fractions (lanes 4 and 6) are IgG heavy chain (55kDa) and light chain (25kDa) and HSA (66kDa) respectively. The goal of depleting these major serum proteins is to increase the relative concentration of the low abundance proteins that are typically masked by these major proteins in the sample. Figure 3 shows an expanded region of a 2 dimensional gel. The enrichment of low intensity protein
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