Spectroscopic studies on copper (II) complexes of human lactoferrin.
The interaction of Cu(II) with human lactoferrin has been studied as a function of pH, using electronic and electron spin resonance spectroscopy. Specific Cu(II) binding, with bicarbonate as the co-anion, occurs over the pH range 6 to 9. In the presence of a fiftyfold molar excess of oxalate, a monocopper(II) lactoferrin oxalate complex forms when the Cu(II) to protein is 1:1. If this ratio is increased to 2:1, a hybrid complex forms, in which the second copper utilizes bicarbonate as the co-anion, thus demonstrating, as for serum transferrin, a difference in the anion binding sites. The quenching of the intrinsic fluorescence of apolactoferrin is significantly less in the presence of oxalate than bicarbonate. The interaction of Cu(II) with apolactoferrin in the presence of the malonate, glycolate, thioglycolate, glycinate, and ethylenediaminetetraacetate ions has been examined.
D001639:Bicarbonates / Q000494:pharmacology; D003300:Copper / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007781:Lactoferrin / Q000378:metabolism*; D007782:Lactoglobulins / Q000378:metabolism*; D011485:Protein Binding
D001639:Bicarbonates; D007782:Lactoglobulins; D003300:Copper; D007781:Lactoferrin