Skip to main content
Article thumbnail
Location of Repository

Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements

By J. Wilting, M.M. Weideman, A.C.J. Roomer and J.H. Perrin


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 ellipticity 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

Topics: Farmacie, albumin, serum albumin, warfarin-albumin, circular dichroism, conformation, N-B transition
Year: 1979
OAI identifier:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • (external link)
  • Suggested articles

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.