[Study of albumin immobilization on synthetic activated charcoal]

The principles of physical and chemical immobilization of 14C-albumin on synthetic carbon sorbents with different physiochemical characteristics and structures are studied with radioisotopic technique. The protein binding to the matrix is shown to occur more tightly in the presence of the activating agent (water soluble carbodiimide). It is marked that the geometric correlation of the protein molecular size and sorbents mezopores dimensions is critical for the effective immobilization. The synthetic spherogranulated CKH carbons are shown to be preferential for biospecific carbon sorbents creation.