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Pilot scale expression and purification of soluble protein A tagged beta 1,6N-acetylglucosaminyltransferase in CHO cells.

Expression of recombinant soluble protein A tagged mouse core 2 beta 6-N-acetylglucosaminyltransferase (E.C. 2.4.1.102) has been scaled-up in CHO cells using a continuously operating fluidized bed system yielding 0.3 U/day. A one step 213 fold purification by affinity chromatography on IgG-Sepharose yielded a stable enzyme preparation with a specific activity of 44 mU/mg. The enzyme was shown to belong to the L-type with a highly restricted specificity for the acceptor substrate Gal beta 1-->3GalNAc alpha 1-->R (core 1). Only little activity towards GlcNAc beta 1-->3Gal-NAc alpha 1-->R (core 3) (< 1%) and no incorporation on unsubstituted benzyl or peptide-bound GalNAc was detected. Zn2+ and to a lesser extent Mn2+ were found to be inhibitory whereas Mg2+ could activate the enzyme. The enzyme preparation proved suitable for in vitro application as a catalyst for the synthesis of core 2 structures.