Summary
Porcine liver β-d-glucose dehydrogenase, a multi-functional protein, has been purified to apparent homogeneity. The enzyme has been separated from the endoplasmic reticulum using Triton X-114 and further purified using NAD to release glucose dehydrogenase from a NADP-linked sepharose column. The purified enzyme is capable of producing both NADH and NADPH in vivo as indicated by kinetic studies.
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Carper, W.R., Groutas, W.C. & Coffin, D.B. Affinity chromatography of glucose dehydrogenase. Experientia 44, 29–32 (1988). https://doi.org/10.1007/BF01960233
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DOI: https://doi.org/10.1007/BF01960233