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. Author manuscript; available in PMC: 2014 Apr 28.
Published in final edited form as: Biochim Biophys Acta. 2013 Apr 8;1830(8):4274–4281. doi: 10.1016/j.bbagen.2013.04.001

Fig. 2.

Fig. 2

Donor specificities of C2GnT2, C2GnT1, C3GnT, and C1GalT. Glycosyl transfer to acceptor substrate was measured as a function of nucleotide sugar donor. Enzymes were assayed as described in the Methods section, except in the presence of different nucleotide sugars replacing the standard donor substrates; 0.40 mM UDP-Gal, 2266 cpm/nmol; 0.345 mM UDP-Glc, 5549 cpm/nmol; 0.5 mM UDP-GlcNAc, 5876 cpm/nmol; or 0.6 mM UDP-GalNAc, 1708 cpm/nmol. The activity with the nucleotide sugar donor specific for each enzyme was set to 100%. C1GalT and C3GnT activities were assayed using GalNAcα-Bn as acceptor substrate; C2GnT1 activity was assayed using Galβ1–3GalNAcα-pnp as acceptor substrate; C2GnT2 activity was assayed using Galβ1–3GalNAcα-pnp and GlcNAcβ1–3GalNAcα-pnp as acceptor substrates.