While immobilized animic textile dyes have been found useful for rapid efficient purification of a variety of proteins, we belive that the utility of these immobilized dyes could be markedly extended to more weakly bound proteins as well as to nucleic acids, subcellular assemblies, membranes and whole cells. Such extension of technology will require quantitative assessment of the contribution of matrices, bridging reagents, immobilized dye concentration, affinity constants and kinetic on/off rates, and pH temperature and solvent polarity. Such measurements will be made on model immobilized dyes as well as on chromatographic columns where feasible. Procedures will also be explored to covalently label protein ligand sites to provide a spectral marker for peptide fragmentation resolution and for kinetic studies of the regeneration of functional ligand binding sites from complementary peptide fragments or from denatured intact polypeptide chains.
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