title: Effect of pH and small inorganic ions on binding of sulfadimethoxine and sulfaphenazole to human serum albumin measured by circular dichroism.
abstract: The binding of sulfadimethoxine and sulfaphenazole to human serum albumin (HSA) has been shown by circular dichroism measurements to be dependent on the N-B transition. The secondary drug binding sites were found to be optically active in the B conformation form in HSA but optically inactive in the N form. Moreover, the drug-HSA interaction in Tris-HCl buffer seems to be more sensitive to the conformational change in HSA, compared with that in the phosphate buffer.
authors.forename: M
authors.initials: M
authors.lastname: Otagiri
authors.forename: H
authors.initials: H
authors.lastname: Nakamura
authors.forename: Y
authors.initials: Y
authors.lastname: Imamura
authors.forename: U
authors.initials: U
authors.lastname: Matsumoto
authors.forename: J
authors.initials: J
authors.lastname: Fleitman
authors.forename: J H
authors.initials: JH
authors.lastname: Perrin
mesh_terms: D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013412:Sulfadimethoxine / Q000097:blood*; D013426:Sulfaphenazole / Q000097:blood*
chemical_list: D012709:Serum Albumin; D013426:Sulfaphenazole; D013412:Sulfadimethoxine