Peptide and carbohydrate complexes of nickel in human kidney.

The predominant renal and urinary forms of nickel consist of low-Mr complexes. Similarities in the nature of these complexes have been found in kidneys of rats exposed parenterally to NiCl2 and in rat kidneys treated with NiCl2 in vitro. Similar complexes have also been identified after treatment of bovine and human renal soluble fractions with NiCl2. The bulk of nickel in all cases is associated with sulphated oligosaccharide fractions containing uronic acids and neutral sugars. This binding is non-specific, and nickel is readily displaced from these fractions by copper. Smaller amounts of nickel are bound to an acidic peptide, which was purified from human kidneys and partially characterized. Nickel was not displaced from this material by copper at physiological pH. These nickel complexes have not been found in plasma, suggesting that ligand exchange occurs during or after glomerular filtration of the metal.