title: Copper complexes at N- and C-site of ovotransferrin: quantitative determination and visible absorption spectrum of each complex.
abstract: Copper complexes at the two sites of ovotransferrin (TF) differed markedly in the rate of Cu release by EDTA. During the reaction, lambda max of the remaining Cu-Tf complex shifted to red side, while the difference spectrum of FenCu2-nTf vs. FenTf in which the N-site had been preferentially occupied with Fe had lambda max at blue side from that of Cu2Tf, 440 nm. From these results, the intrinsic spectrum for Cu-complex at each site was assigned: lambda max 450 nm for N- and 430 nm for C-site. The differences in the release rate and the spectrum can be used for the identification of the two domains of Tf and for the analysis of metal-binding behavior of each site.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003207:Conalbumin / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004527:Egg Proteins / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D008345:Manganese; D013053:Spectrophotometry
chemical_list: D004527:Egg Proteins; D003207:Conalbumin; D008345:Manganese; D003300:Copper; D004492:Edetic Acid; D007501:Iron