Chloride ion nuclear magnetic resonance spectroscopy probe studies of copper and nickel binding to serum albumins.
The binding of Cu2+ and Ni2+ to bovine, dog, and human serum albumin has been studied by the 35Cl NMR probe technique. The number of primary copper sites were estimated to be 1.3 for human serum albumin, 3.1 for bovine serum albumin, and 6.6 for dog serum albumin. A similar number of primary nickel sites was determined for each of these albumins. On the basis of the chloride probe experiments, it appears that both copper and nickel have the same binding sites on albumin.
D000818:Animals; D002417:Cattle; D002712:Chlorides / Q000097:blood*; D003300:Copper / Q000097:blood*; D004285:Dogs; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009532:Nickel / Q000097:blood*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism
D002712:Chlorides; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D003300:Copper; D009532:Nickel