Abstract
(1) Copper complexes at the two sites of ovotransferrin (Tf) differed markedly in the rate of Cu release by EDTA. (2) During the reaction, λ max of the remaining Cu-Tf complex shifted to red side, while the difference spectrum of Fe nCu 2−nTf vs. Fe nTf in which the N-site had been preferentially occupied with Fe had λ max at blue side from that of Cu 2Tf, 440 nm. (3) From these results, the intrinsic spectrum for Cu-complex at each site was assigned: λ max 450 nm for N- and 430 nm for C-site. (4) 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.
Published Version
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