The specific binding of iron (III) and copper (II) to transferrin and conalbumin
R Aasa, BG Malmström, P Saltman… - Biochimica et biophysica …, 1963 - Elsevier
The binding of Fe 3+ to transferrin has been studied by pH titrations and equilibrium dialysis.
In the pH range studied (7.5–8.9), 3 H+ are released for each Fe 3+ bound. In the dialysis
experiments, EDTA and citrate were used as competing chelating agents. It was found that
the binding of Fe 3+ to transferrin may be described as coordination to two equivalent and
independent sites. The nature of the binding sites in transferrin as well as conalbumin has
been studied by measurements of ESR and visible spectra. The ESR spectra of the Fe …
In the pH range studied (7.5–8.9), 3 H+ are released for each Fe 3+ bound. In the dialysis
experiments, EDTA and citrate were used as competing chelating agents. It was found that
the binding of Fe 3+ to transferrin may be described as coordination to two equivalent and
independent sites. The nature of the binding sites in transferrin as well as conalbumin has
been studied by measurements of ESR and visible spectra. The ESR spectra of the Fe …