Figure 3.

Purification and deglycosylation of recombinant RoGAs. (A) Purified proteins (1 μg) obtained by cation-exchange chromatography were subjected to electrophoresis on a 15% SDS-PAGE and stained with Coomassie Brilliant Blue R-250. Lane 1, full-length GA; lane 2, GAΔ168–604; lane 3, GAΔ132–604; lane 4, GAΔ26–131; lane 5, GAΔ26–145 and lane 6, GAΔ26–160. (B) Protein samples were treated with PNGase F (250 U) and resolved by 10% SDS-PAGE. Symbols (+) and (-) indicate treatment with and without PNGase F, respectively. (C) Recombinant SBD was treated with Jack bean α-mannosidase and examined by 15% SDS-PAGE. Symbols (+) and (-) indicate treatment with and without Jack bean α-mannosidase, respectively.

Lin et al. BMC Biochemistry 2007 8:9   doi:10.1186/1471-2091-8-9
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