The N-terminal lobe fragment of hen ovotransferrin was prepared by trypsin digestion and the following gel filtration and ion-exchange chromatography. EPR spectra of Cu(II) complex of the N-terminal fragment were recorded independently from the C-terminal lobe and a major spectrum of the copper(II) complex showed g∥ = 2.300 and g⊥ = 2.061 with ACu∥ = 14.0 mT, ACu⊥ = 2.20 mT, which had a superhyperfine splitting (AN⊥ = 1.44 mT) of a nitrogen ligand, which may correspond to type A-1 site of copper binding position in the N-terminal lobe of hen ovotransferrin.
|Number of pages||2|
|Publication status||Published - 2001|
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