AFFINITY CHROMATOGRAPHY FOR THE DINUCLEOTIDE FOLD

虽然已经发现固定化的动物纺织品染料可用于快速合成， 高效纯化各种蛋白质，我们相信， 这些固定化染料可以显着扩展到更弱的结合 蛋白质以及核酸、亚细胞组装体、膜和 全细胞 这种技术的扩展将需要定量的 基质、桥接试剂、固定化 染料浓度、亲和常数和动力学开/关速率以及pH 温度和溶剂极性。 这些测量将在模型上进行 固定化染料以及在可行的情况下在色谱柱上。 程序也将探讨共价标记蛋白质配体网站 提供用于肽片段化解析的光谱标记， 再生功能性配体结合位点的动力学研究 互补肽片段或来自变性的完整多肽链。

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.