The article is devoted to the theoretical aspects of the development of the effective method for the removal of protein-bound uremic toxins. It is shown that the methods of flow and differential scanning microcalorimetry are sufficient enough for the evaluation of the degree of ligand loading of human serum albumin with protein-bound uremic toxins. The molecules of albumin isolated from blood plasma of the patients being kept on chronic dialysis are demonstrating significant alterations of conformation and complex-forming properties, the correction of which by conventional methods of extracorporeal detoxification (exhaustive dialysis, treatment on synthetic SCN carbons) are practically ineffective. Deliganding of uremic albumin may be successfully performed on conventional carbon haemosorbents upon preliminary separation of blood plasma and its dilution with acetate buffer 1:1 at pH = 5.08. Treatment of the whole blood of patients onto new mass-fractal deliganding carbon, i.e., hemosorbents of HSGD trademark. These HSGD haemosorbents quite effectively could be used for restoration of main parameters of uremic HAS molecules conformation and ligand-binding activity simultaneously with hemodialysis upon the protection by locally performed citrate anticoagulation as an easier and cheaper method for the removal of protein-bound uremic toxins.