title: Characterization of the binding of Triton X-100 to equine and rabbit serum albumin.
abstract: The binding isotherms for Triton X-100 binding to equine and rabbit serum albumin were determined by equilibrium dialysis at 16 degrees C in pH 7.0, I = 0.05 phosphate buffer. Presented in a Scatchard plot, the binding isotherms are a straight line, indicating thermodynamically independent and identical binding sites. In this model equine serum albumin is characterized as having 11 such sites with an equilibrium constant of 6.0 x 10(3) M-1. Similarly, rabbit serum albumin is characterized as having 9 such sites with an equilibrium constant of 8.0 x 10(3) M-1.
mesh_terms: D000818:Animals; D003902:Detergents; D006736:Horses; D007700:Kinetics; D017830:Octoxynol; D011092:Polyethylene Glycols; D011485:Protein Binding; D011817:Rabbits; D012709:Serum Albumin; D013045:Species Specificity; D013501:Surface-Active Agents; D013816:Thermodynamics
chemical_list: D003902:Detergents; D012709:Serum Albumin; D013501:Surface-Active Agents; D011092:Polyethylene Glycols; D017830:Octoxynol