RESUMO
The problem of interaction of human serum albumin (HSA), unconjugated bilirubin (UB) and high porosity activated HSGD carbons is investigated in this study. The decrease of UB to HSA molecular ratio by more than 300 times was demonstrated while the batch experiments in HSA-UB admixtures after contact with HSGD. HSGD carbons express extremely high activity for the removal of UB from HSA containing solutions (more than 100 mg of UB per 1 g of activated carbon). Ex-tempore albumin-coating of carbon surface decreases adsorbent capacity by bilirubin on 21%. At the same time ex-tempore albumin-coating of HSGD carbon surface as well as blood citratization prevent platelet and leukocytes loss and clotting inside of the column. Pharmacopoeia solution of HSA containing acetyl-tryptophan or octanoate used for albumin-coating of HSGD adsorbents, becomes ligand-free and rather more active in complexing with protein-bound substances. Combination of albumin-coated HSGD carbon as haemosorbent with HSA ligand-free solution as a transfusion media seems a new prospective modality of the extracorporeal removal of protein-bound toxins.
