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Figure 1 | BMC Biochemistry

Figure 1

From: Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis

Figure 1

BDH purification steps from jerboa liver. Proteins (40 μg) were resolved by SDS-PAGE and stained with Coomassie Brilliant Blue (a) or subjected to Western blot (b) using the purified polyclonal anti-BDH antibodies. Lanes M, 1, 2, 3, 4, and 5 represent standard proteins, crude extract, 30–50% ammonium sulphate fraction, phenyl-Sepharose fraction, affinity chromatography fraction, and immunoaffinity chromatography eluate pool (pure protein preparation). Bound antibody was located by immunoreaction combined with peroxidase conjugated goat anti-rabbit IgG. The arrow (b) indicates the band corresponding to the BDH subunit.

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BMC Biochemistry

ISSN: 1471-2091

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