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. 2009 Jan 7;9(1):23–34. doi: 10.1016/j.cmet.2008.11.008

Figure 1.

Figure 1

Studies on Binding of Glycogen to Bacterially Expressed β1-GBD

(A) Binding of GST:GBD fusion, free GST, and phosphorylase a to glycogen. Samples of each protein were incubated with bovine or rat liver glycogen bound to ConA-Sepharose, the Sepharose beads were recovered by centrifugation, and samples of the load (L), supernatant (S), and pellet (P, resuspended in the original volume) were analyzed by SDS-PAGE.

(B) Alignment of GBD sequences from various eukaryotes made using ALIGNX. Residues identical in all species are boxed, as are conserved residues in mammalian species directly involved in carbohydrate binding; the latter are identified at the bottom (rat β1 numbering).

(C) Binding to glycogen of GST:GBD fusions (wild-type rat β1 or the point mutations shown). The binding assay was as in (A) using bovine liver glycogen, and binding of phosphorylase a was analyzed as a positive control (bottom panel).