Copper complexes at N- and C-site of ovotransferrin: quantitative determination and visible absorption spectrum of each complex.
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.
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
D004527:Egg Proteins; D003207:Conalbumin; D008345:Manganese; D003300:Copper; D004492:Edetic Acid; D007501:Iron