Efficiency of the affine sorbent based on N-vinylpyrrolidone and maleic anhydride for the plasminogen isolation from human blood plasma depends on fixed structural immobilization of L-lysine to the polymer matrix under consideration. This specificity of structure is caused by covalent binding of L-lysine to the polymer matrix only by an <$E alpha>-aminogroup while the <$E epsilon>-arninogroup of L-lysine remains in the basic form. The last is achieved by the blocking of <$E epsilon>-aminogroups in the basic form by the interaction with benzaldehyde, i. e. by the formation of a Schiff base, and by binding the <$E alpha>-aminogroup of L-lysine into a copper complex.

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