Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements.
The molar ellipticity of the warfarin-albumin complex at 310 nm increases with pH from 6 to 9. This pH dependence runs parallel with that of the molar ellipticity of the albumin alone at 292 nm. The change in molar ellipicity with pH occurs in a smaller pH interval after addition of the physiological concentration of calcium ions. These findings give support to the assumption that the binding site for warfarin on the albumin molecule is affected by the neutral-to-base transition in the protein.
D001665:Binding Sites; D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism; D014859:Warfarin / Q000097:blood
D012709:Serum Albumin; D014859:Warfarin