AFFINITY CHROMATOGRAPHY FOR THE DINUCLEOTIDE FOLD

而固定化的动物纺织品染料被发现对快速 高效纯化多种蛋白质，我们相信其实用价值 其中的固定化染料可以显著地扩展到更弱的结合 蛋白质以及核酸、亚细胞组件、膜和 整个细胞。这种技术扩展将需要量化 固定化的基质、桥接剂的贡献的评估 染料浓度、亲和常数和动力学开/关速率，以及pH 温度和溶剂的极性。这样的测量将在模型上进行 固定化染料以及在可能的情况下在色谱柱上。 还将探索共价标记蛋白质配体位点的程序 为多肽裂解提供光谱标记物 功能配体结合部位再生的动力学研究 互补的多肽片段或来自变性完整的多肽链。

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.