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. 2012 Aug 27;7(8):e43828. doi: 10.1371/journal.pone.0043828

Figure 1. Schematic domain structures (A) and SDS-PAGE analysis (B) of the non-GH proteins and glycoside hydrolases.

Figure 1

A: A schematic representation of the polypeptides of CbHsp18, MkHistone1, and the three glycoside hydrolases of C. bescii used in this study. GH9: Glycoside hydrolase family 9 domain; CBM3c: Carbohydrate binding module family 3 type C. B: SDS-PAGE analysis of purified recombinant non-GH proteins and the three glycoside hydrolases of C. bescii. Lane 1: molecular mass markers; lane 2: CbHsp18; lane 3: MkHistone1; lane 4: RNase A; lane 5: CbCelA-TM1; lane 6: CbCdx1A; lane 7: CbXyn10A. Two micrograms of each protein were resolved by 12% SDS-PAGE. RNase A was a commercial product (Roche).