1/T1 NMRD profiles of solutions of Mn2+ and Gd3+ protein-chelate conjugates.
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.
D001665:Binding Sites; D002614:Chelating Agents; D003287:Contrast Media; D005682:Gadolinium; D007136:Immunoglobulins; D009682:Magnetic Resonance Spectroscopy; D008345:Manganese; D011506:Proteins; D012710:Serum Albumin, Bovine
D002614:Chelating Agents; D003287:Contrast Media; D007136:Immunoglobulins; D011506:Proteins; D012710:Serum Albumin, Bovine; D008345:Manganese; D005682:Gadolinium