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Binding of various mercurial compounds to serum proteins

Journal Article · · Bull. Environ. Contam. Toxicol.; (United States)
DOI:https://doi.org/10.1007/BF01686202· OSTI ID:7240315
Binding study of /sup 203/Hg-labeled Hg/sup 2 +/, phenylmercuric acetate (PMA), methylmercuric chloride (MMC) and ethylmercuric chloride (EMC) to serum albumin of six mammalian species, bovine hemoglobin and bovine ..gamma..-globulin is presented. Both MMC and EMC bound only weakly to serum albumin and ..gamma..-globulin and more strongly to hemoglobin; Hg/sup 2 +/ bound very strongly to both albumin and hemoglobin and weakly to ..gamma..-globulin; and PMA bound most strongly to albumin, next to hemoglobin, and the least to ..gamma..-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.
Research Organization:
Oregon State Univ., Corvallis
OSTI ID:
7240315
Journal Information:
Bull. Environ. Contam. Toxicol.; (United States), Journal Name: Bull. Environ. Contam. Toxicol.; (United States) Vol. 15:1; ISSN BECTA
Country of Publication:
United States
Language:
English