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Titlebook: Immobilized Biochemicals and Affinity Chromatography; R. Bruce Dunlap Book 1974 The Editor(s) (if applicable) and The Author(s), under exc

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Affinity Chromatography — Old Problems and New Approacheso a wide variety of problems is comparatively recent. As long ago as 1910 there were reports of the purification of amylase by adsorption to insoluble starch (2). Tyrosinase was purified in 1953 using a cellulose matrix bearing the inhibitor, diazodizine (3). In both of these examples the power of p
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Non-Specific Binding of Proteins by Substituted Agarosesely charged but unrelated proteins invariably were strongly bound by agarose (Sepharose 4B) substituted with an n-alkylamine or with 4-phenyl-n-butylamine (PBA).. Un-substituted agarose or agarose treated with CNBr, but without subsequent addition of amine, did not bind these proteins. Positively ch
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A Solid Phase Radioimmune Assay for Ornithine Transcarbamylase by Yalow and Berson (1960) is based on the ability of unlabeled antigen to compete with antigen labeled with a radioactive isotope bound to antibody. After permitting the system to reach equilibrium antibody bound radioactivity was separated from unbound radioactivity and one or the other determine
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Affinity Chromatography of Thymidylate Synthetases Using 5-Fluoro-2′-Deoxyuridine 5′-Phosphate Derivthylenetetrahydrofolate donates its labile one-carbon unit (the methylene group) to deoxyuridylate, and also provides the reducing power necessary to convert the methylene group to methyl leading to the formation of thymidylate and dihydrofolate, as is shown in equation (1). The dihydrofolate so for
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