Brodersen R, Honoré B, Larsen F G
Acta Pharmacol Toxicol (Copenh). 1984 Feb;54(2):129-33. doi: 10.1111/j.1600-0773.1984.tb01906.x.
The shape of binding isotherms for sixteen ligands to human serum albumin showed no signs of approaching saturation at high ligand concentrations. It is suggested that ligand binding to serum albumin is essentially different from saturable binding of substrates to enzymes, of oxygen to haemoglobin, etc. Binding to serum albumin appears to be non-saturable.
16种配体与人血清白蛋白的结合等温线形状表明，在高浓度配体时没有接近饱和的迹象。这表明配体与血清白蛋白的结合本质上不同于底物与酶、氧与血红蛋白等的可饱和结合。与血清白蛋白的结合似乎是不饱和的。
