Biomedical Engineering Reference
In-Depth Information
Membrane Chromatography
Purification of proteins from complex mixtures is a key process in pharma-
ceutical research and production. But chromatography based on particu-
late matrices involves lengthy procedures and separation times. Sartobind
SingleSep® ion exchange capsules are designed to remove contaminants from
therapeutic proteins at accelerated flow rates. This is a direct result of negligible
mass transfer effects and is made possible by the >3 μm macroporous mem-
brane. The design allows for robust chromatographic separations and drasti-
cally reduced validation costs. Sartobind SingleSep capsules are designed to
remove charged contaminants from therapeutic proteins at accelerated flow
rates by ion exchange membrane chromatography. The high throughput is a
direct result of negligible mass transfer effects and is made possible by the >3
μm macroporous membrane with 4 mm (15 layer) bed height.
Sartobind replaces time-consuming tedious chromatographic steps for
many protein and virus applications. The rapid purification on Membrane
Adsorbers allows the isolation of protein with high yield up to 100 faster
than conventional columns at a flow rate of 20 to 40 bed volumes per minute.
(See Figure 8.1.)
The micrograph (
Figure 8.2
) shows some chromatographic gel beads (aver-
age particle size 90 µm) on the surface of the Sartobind Membrane Adsorber.
Even at 500-fold magnification, pores of beads are invisible, but the mem-
brane displays a wide pore structure of 3-5 µm size.
Conventional beads keep more than 95% of the binding sites inside the par-
ticle. In Sartobind membranes, the binding sites are grafted homogenously
as an approximately 0.5-1 µm film on the inner walls of the reinforced and
FIGURE 8.1
Schematic view of viruses binding to functional groups in the membrane pores.
