Conclusion
The expression and purification of soluble human DP IV was established in P. pastoris on a 5 liter fermentation scale (3 mg/fermentation, 32.27 U/mg). Thus it represents an alternate approach to previous published methods were DP IV was expressed in cell culture (Tanaka et al.7) with lower production rates and to the production in insect cells (Dobers et al.8) Biochemical and kinetic characterization demonstrated that the soluble recombinant DP IV displayed similar properties as DP IV purified from porcine kidney regarding size, activity, isoelectric point and glycosylation. Furthermore, the new expression method enables future structure-function related studies of DP IV.
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Baer, J.W., Gerhartz, B., Hoffmann, T., Rosche, F., Demuth, HU. (2004). Characterisation of Human DP IV Produced by a Pichia pastoris Expression System. In: Back, N., Cohen, I.R., Kritchevsky, D., Lajtha, A., Paoletti, R. (eds) Dipeptidyl Aminopeptidases in Health and Disease. Advances in Experimental Medicine and Biology, vol 524. Springer, Boston, MA. https://doi.org/10.1007/0-306-47920-6_13
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DOI: https://doi.org/10.1007/0-306-47920-6_13
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