Lauffer R B, Brady T J, Brown R D, Baglin C, Koenig S H
Magn Reson Med. 1986 Aug;3(4):541-8. doi: 10.1002/mrm.1910030407.
Bovine immunoglobulins (IgG) and bovine serum albumin (BSA) were multiply labeled with multidentate ligands, either ethylenediaminetetraacetic acid (EDTA) or diethylenetriaminepentaacetic acid (DTPA), and metal ions were inserted to form the ternary protein-ligand-ion conjugates. The NMRD profiles (the magnetic field dependence of 1/T1) of solutions of the ternary conjugates differ greatly from those of the corresponding binary ligand-metal-ion complexes, both in magnitude and functional form, exhibiting 5- to 10-fold greater relaxivities and prominent peaks near 20 MHz. The inference is that the protein-bound chelates are relatively rigidly attached to the macromolecules. The structure and metal ion affinities of these novel conjugates, as well as the relevance to contrast enhancement in NMR imaging, is discussed.
牛免疫球蛋白（IgG）和牛血清白蛋白（BSA）用多齿配体进行多重标记，这些配体可以是乙二胺四乙酸（EDTA）或二亚乙基三胺五乙酸（DTPA），然后插入金属离子以形成三元蛋白质-配体-离子共轭物。三元共轭物溶液的NMRD图谱（1/T1对磁场的依赖性）在大小和功能形式上都与相应的二元配体-金属-离子络合物有很大不同，其弛豫率高5至10倍，并且在20 MHz附近有突出的峰。由此推断，与蛋白质结合的螯合物相对牢固地附着在大分子上。本文讨论了这些新型共轭物的结构和金属离子亲和力，以及它们与核磁共振成像中对比度增强的相关性。
