Assessing the scalability of dynamic field gradient focusing by linear modeling

Journal of Separation Science
Noah I Tracy, Cornelius F Ivory

Abstract

Dynamic field gradient focusing (DFGF) separates and concentrates proteins in native buffers, where proteins are most soluble, using a computer-controlled electric field gradient which lets the operator adjust the pace and resolution of the separation in real-time. The work in this paper assessed whether DFGF could be scaled up from microgram analytical-scale protein loads to milligram preparative-scale loads. Linear modeling of the electric potential, protein transport, and heat transfer simulated the performance of a preparative-scale DFGF instrument. The electric potential model showed where the electrodes should be placed to optimize the shape and strength of the electric field gradient. Results from the protein transport model suggested that in 10 min the device should separate 10 mg each of two proteins whose electrophoretic mobilities differ by 5 x. Proteins with electrophoretic mobilities differing by only 5% should separate in 3 h. The heat transfer model showed that the preparative DFGF design could dissipate 1 kW of Joule heat while keeping the separation chamber at 25 degrees C. Model results pointed to DFGF successfully scaling up by 1000 x using the proposed instrument design.

References

Jun 13, 1998·Biotechnology Progress·R D Greenlee, C F Ivory
Jun 4, 2002·Analytical and Bioanalytical Chemistry·Qinggang WangMilton L Lee
Jan 27, 2004·Electrophoresis·Cornelius F Ivory
Sep 10, 2004·Journal of Chromatography. a·P Myers, K D Bartle
Nov 10, 2005·Journal of Separation Science·Ryan T Kelly, Adam T Woolley
Jan 25, 2007·Electrophoresis·Cornelius F Ivory
May 8, 2007·Journal of Chromatography. a·Paul H HumbleMilton L Lee
Jan 1, 2007·Biochemistry and Molecular Biology Education : a Bimonthly Publication of the International Union of Biochemistry and Molecular Biology·Judith G Voet, Donald Voet

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