In this paper was studied the interaction of deutero- and hematoporphyrin with bovine serum albumin, using various methods of physico-chemical analysis. It was established that the localization of porphyrins occurred in the IB subdomain, while hematoporphyrin interacted with the protein in a monomeric form, and deuteroporphyrin - as a J-dimer. Based on spectral studies, the affinity constants of binding albumin with porphyrins were determined, and the affinity of the protein for deuteroporphyrin appeared to be higher than for hematoporphyrin. It was shown that the interaction of albumin with the studied porphyrins led to a change in the secondary structure of the protein, it being accompanied by a decrease in the proportion of disordered protein fragments and an increase in β-folding.
