Zero-field Mössbauer studies of diferric human transferrin.
Diferric transferrin samples labelled with 57Fe at the N- or the C-terminal binding sites are compared by Mössbauer spectroscopy at 15 K and in zero magnetic field. The spectra of the samples are similar but the fitting of single Lorenzian lines to the data shows that some of the line positions differ in the two cases. According to this we can not exclude a difference between the chemical structures of the binding sites that can arise for example from the participation of different forms of the anion and/or water in the two lobes of transferrin. All other line parameters (line-width, intensity) are the same within the limits of errors.
Kilár
F
F
Department of Physics, Uppsala University, Sweden.
Seidel
A G
AG
Häggström
L
L
D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000378:metabolism; D007503:Iron Isotopes; D015204:Spectroscopy, Mossbauer; D014168:Transferrin / Q000378:metabolism
D007503:Iron Isotopes; D014168:Transferrin; C028283:diferric transferrin; D007501:Iron