Abstract
Bovine serum albumin (BSA) was continuously desalted from alkaline salts (a mixture of sodium phosphate, sodium chloride and potassium chloride) using a size-exclusion gel as the stationary phase. An annular chromatograph was used to achieve a continuous mode of operation and therefore a reasonable throughput. Distribution and mass transfer coefficients of the substances as well as bed properties were obtained by batch chromatography. These separations were simulated mathematically applying an approximate linear chromatographic theory. It was shown experimentally and theoretically that the BSA and the salt solution could be recovered continuously in a purity higher than 98%. The influence of rotation rate on the resolution of the individual peaks was investigated.
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