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. Author manuscript; available in PMC: 2012 Oct 5.
Published in final edited form as: Bioconjug Chem. 2009 Mar 18;20(3):608–618. doi: 10.1021/bc800534r

Figure 4.

Figure 4

(A) The catalytic activities of the α3Gal-T mutants 280SGG282 (○) and 280AGG282 (●) with UDP-GalNAc as the donor substrate at different concentrations of lactose. The insert shows the catalytic activity of the wild-type α3Gal-T with UDP-Gal as the sugar donor at different concentrations of lactose. Each assay was carried out for 15 min with 1 µg of enzyme, as described in Materials and Methods. (B) Time course of GalNAc transfer with 1 µg of mutant enzymes 280SGG282 (○) and 280AGG282 (●) at 200 mmol lactose and 500 µmol UDP-GalNAc.