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Affinity binding of a vampire bat plasminogen activator to SEC resins
M T McCaman1, C Souders, S Ottoboni
1Process Development Department, Berlex Biosciences, 15049 San Pablo Avenue, Richmond, California 94804-00990, USA. mike_mccaman@berlex.com
Protein Expression and Purification
|March 14, 1998
Abstract:
DSPAalpha1 is a recombinant form of the vampire bat plasminogen activator which we have produced in mammalian cell culture. During the development of a recovery process for DSPAalpha1 we observed an unexpected binding interaction between this protein and several types of gel filtration chromatography resins. Under typical operating conditions using neutral pH buffers, we found that DSPA flows through the sizing resin and is fractionated, as expected, according to its molecular size. However, DSPA applied under certain acidic conditions (