Relaxation rates in aqueous solutions containing 30-100 µM heparin as well as 150 µM GBCA were measured as a function of time. Different ZnCl2 stimuli with concentrations between 0.125-4 mM were used as competing ions that initiate a transmetallation and a transchelation process of the Gd3+ ion from GBCAs to glycosaminoglycans. The time resolved relaxometry measurements indicate that glycosaminoglycans play a concentration-dependent double role as competing chelator structures. They foster the thermodynamic instability of intact GBCA by sequestering Gd3+ from the contrast agent but simultaneously interact with competing ions and thus cause a reduced kinetic instability.
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