title: Thyroxine binding properties of glycosylated bovine serum albumin.
abstract: Thyroid hormone, thyroxine (T4) binding properties of glycosylated bovine serum albumin (G-BSA), and intact BSA were studied by the fluorescence method. The apparent binding constants for intact BSA were 0.8 (0.16) x 10(6) M-1 at pH 5.0 and 2.18 (0.06) x 10(6) M-1 at pH 9.5 at 25 degrees C. T4 binding for G-BSA was independent of pH and the apparent binding constant was 1.4 x 10(6) M-1. Thermodynamic parameters were also evaluated from the Van't Hoff plots of the apparent binding constants at pH 7.4 and 8.5. At both pH's, the free energy, enthalpy and entropy changes were almost the same for both G-BSA and BSA.
authors.affiliation: Faculty of Pharmaceutical Sciences, Kinki University, Osaka, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Okabe
authors.forename: M
authors.initials: M
authors.lastname: Hokaze
mesh_terms: D000818:Animals; D002417:Cattle; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013974:Thyroxine / Q000097:blood / Q000737:chemistry*
chemical_list: D012710:Serum Albumin, Bovine; D013974:Thyroxine