[Soluble complexes of bovine serum albumin with linear polyelectrolytes].

Interaction of bonive serum albumin with copolymers 2-methyl-5-vinylpyridine, acrylic and methacrylic acids in different proportions in aqueous solutions was studied. It was shown, that in a wide range of ration of the components soluble cooperative complexes were formed. Ability of amphotheric copolymers to form complexes with bovine serum albumin depend both on the composition of the copolymers and on the pH of the medium. The non-polar interactions of the protein globules with hydrocarbonic 2-methyl-5-vinylpyridine chain fragments of the polyampholyte play an important role in the association of similarly charged particals. It was shown that besides this effect of chain fragments of 2-methyl-5-vinylpyridine a significant contribution in the association is made by non-polar interactions, created by methyl groups in copolymer 2-methyl-5-vinylpyridine and methacrylic acid. The association mechanism and structure of the formed complexes was studied. It was shown that complex formation is accompanied by non-equal distribution of the chain copolymer between the protein globules and appearance of asymmetric particles of the complex. A correlation between the ability of polyampholytes to bind protein and their physiological action was found.