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Fig. 1 | AMB Express

Fig. 1

From: Purification and characterization of a novel glutamate dehydrogenase from Geotrichum candidum with higher alcohol and amino acid activity

Fig. 1

The elution profiles for the GDH extracts. Asterisk Indicates the fraction with a hexanol, glutamate, and α-ketoglutarate activity. The ammonium sulphate precipitated material was fractionated by ion-exchange (a); and the most active peaks were separated by gel filtration (b); the main active peak was further analyzed for purity by HPLC (c). The native-PAGE analysis showed the most active peak from the above steps (d, e) is lane M. Lane M. Native molecular mass marker, Lane 1. Purified GDH on gel filtration. Lane 2. Peak 4 from the gel filtration. Lane 3. Crude enzyme. The gel in (d) is stained with coomassie brilliant blue and the gel in (e) is stained with dehydrogenase active staining solution with hexanol as a substrate. The SDS-PAGE analysis shows the most active peak from the above steps (f): Lane M. Molecular mass marker, Lane 1. Purified GDH on Gel filtration. See “Materials and methods” for more details on the purification methods

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