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- W2011845539 abstract "An affinity column was synthesized and utilized to partially purify glycerolphosphate dehydrogenase (L-glycerol-3-phosphate: NAD+ oxidoreductase, E.C.1.1.1.8) from rat skeletal muscle. The novelty of the column resides in the fact that the ligand used, 6-phosphogluconic acid, is neither an inhibitor nor a substrate of the enzyme when free in solution but when immobilized on an agarose matrix, glycerol phosphate dehydrogenase binds to it with a high degree of specificity. The bound enzyme could be eluted by either increasing the ionic strength or by addition of its natural substrate, α-glycerol phosphate. Using a combination of these methods and ammonium sulfate precipitation GPDH was purified about 250 fold with a 75% yield within 24 hours." @default.
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- W2011845539 date "1974-09-01" @default.
- W2011845539 modified "2023-10-18" @default.
- W2011845539 title "A novel affinity column for purification of glycerol phosphate dehydrogenase" @default.
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- W2011845539 doi "https://doi.org/10.1016/0006-291x(74)90190-9" @default.
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