The binding of various mercurial compounds to serum proteins

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Abstract
Binding study of Hg-labeled Hg2+, PMA, MMC and EMC to serum albumin of six mammalian species, bovine hemoglobin and bovine γglobulin is presented. Both MMC and EMC bound only weakly to serum albumin and γ-globulin and more strongly to hemoglobin; Hg2+ bound very strongly to both albumin and hemoglobin and weakly to γ-globulin; and PMA bound most strongly to albumin, next to hemoglobin and the least, to γ-globulin. The available binding sites varied from one to five per molecule of protein. Human serum albumin has the lowest association constants with all four mercurial compounds, indicating that it was not as tightly bound to mercurial compounds as found with serum albumins from other species.