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Fig. 3 | Annals of Microbiology

Fig. 3

From: Characterization of β-galactosidase and α-galactosidase activities from the halophilic bacterium Gracilibacillus dipsosauri

Fig. 3

Nondenaturing gel electrophoresis of G. dipsosauri strain DD1 samples after staining with X-β-Gal and X-α-Gal. Samples (10 μl) were combined with nondenaturing sample buffer (10 μl) and separated in a 12-well 4–15% Tris-glycine gel. Samples were as follows: (1) PM2500 molecular markers; (2) desalted P80 fraction; (3) protein pool from MacroPrep DEAE column containing β-galactosidase I activity; (4) fraction 22 from the Sephadex G-200 column using this pool; (5) protein pool from the MacroPrep DEAE column containing β-galactosidase II activity and some α-galactosidase activity; (6) fraction 23 from the Sephadex G-200 column using this pool; (7) protein pool from the MacroPrep-DEAE column containing α-galactosidase activity and some β-galactosidase activity; (8) fraction 21 from the Sephadex G-200 column using this pool; (9) protein pool from the MacroPrep DEAE column containing β-galactosidase II activity and some α-galactosidase activity; (10) fraction 23 from the Sephadex G-200 column using this pool; (11) protein pool from the MacroPrep-DEAE column containing α-galactosidase activity and some β-galactosidase activity; and (12) fraction 21 from the Sephadex G-200 column using this pool. After electrophoresis, the gel was divided into two parts: the part with lanes 1 to 8 was stained with X-β-Gal and the part with lanes 9 to 12 was stained X-α-Gal. The two parts were pushed back together prior to photography. Because of washing and processing, only the red-stained band at 75 kDa in the molecular marker mixtures was clearly visible. The positions of the other markers in lane 1 are indicated in the text box on the left

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