[The role of oligomeric structure of human serum albumin during its interaction with polyalbumin receptors in blood serum of patients with viral hepatitis B].

Several oligomers of human blood serum albumin modified by glutaraldehyde differ in their binding ability to polyalbumin receptors in blood serum of patients with viral hepatitis B. Erythrocytes containing the albumin tetramer are able to agglutinate, while the red blood cells coated with dimer or monomer are deprived of this property. At the same time, the albumin dimers and monomers neutralize agglutination of the erythrocytes containing the complete pool of modified albumin in membranes although their effect is distinctly lower than that of tetramer. The albumin tetramer may have two or more sites of binding to erythrocytes or to the surface antigen of hepatitis B virus, bearing polyalbumin receptors, whereas the protein dimer or monomer contained only one site of binding.