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- W61875669 abstract "The affinity chromatography of enzymes is reviewed in terms of the operational capacity of the ligand. Many group'specific ligands function in a rather inefficient manner. Reasons for this inefficiency are examined and the apparent KAs calculated from frontal analysis data. The effect of changing the support matrix is presented as well as the variation of the latter with ligand concentration. The direct relation between the capacity and apparent KA is also shown. On the other hand, the capacities of two triazine-linked dyes, Procion Red and Cibacron Blue, are mugh higher than those of nucleotides. Cibacron Blue columns seem more effective in binding NAD +-dependent dehydrogenases whilst Procion Red columns are better suited to the purification of NADP +-dependent dehydrogenases. Yeast extract enzymes are separable using both blue and red columns with quite different elution profiles. The red column has been used to purify glutamate dehydrogenase from N. crassa. A novel method for the purification of L. casei dihydrofolate reductase on NADPH-Sepharose is described. A new method for the preparative electrophoretic desorption of proteins from affinity matrices and immunoadsorbents is illustrated." @default.
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- W61875669 date "1978-01-01" @default.
- W61875669 modified "2023-09-23" @default.
- W61875669 title "AFFINITY CHROMATOGRAPHY OF ENZYMES" @default.
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- W61875669 doi "https://doi.org/10.1016/b978-0-08-022632-3.50006-4" @default.
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