The binding of various mercurial compounds to serum proteins.
Binding study of 203Hg-labeled Hg2+, PMA, MMC and EMC tp serum albumin of six mammalian species, bovine hemoglobin and bovine lambda-globulin is presented. Both MMC and EMC bound only weakly to serum albumin and lambda-globulin and more strongly to hemoglobin; Hg2+ bound very strongly to both albumin and hemoglobin and weakly to lambda-globulin; and PMA bound most strongly to albumin, next to hemoglobin and the least, to lambda-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.
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D005035:Ethylmercury Compounds / Q000378:metabolism; D006736:Horses; D006801:Humans; D008628:Mercury / Q000378:metabolism*; D008631:Mercury Radioisotopes; D008767:Methylmercury Compounds / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits; D012709:Serum Albumin / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012756:Sheep; D013552:Swine
D001798:Blood Proteins; D005035:Ethylmercury Compounds; D008631:Mercury Radioisotopes; D008767:Methylmercury Compounds; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D008628:Mercury