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- W2018910615 abstract "1.Human ceruloplasmin was prepared from two different Cohn fractions and from fresh serum. The EPR spectrum, the total electron-accepting capacity and the optical and potentiometric titration behavior of the preparations were studied and compared. 2.Although the preparations had undergone hydrolytic attack to a very different degree, no significant difference in the properties mentioned was found. Only the rate, at which electrons were taken up by the protein in anaerobic experiments, was found to vary with the preparation. 3.The EPR spectra indicated that in addition to two Type I Cu2+, the protein contained only one Type 2 ion, with an EPR spectrum being affected by the presence of azide. 4.In agreement with previous reports, the number of electrons the protein can accept equals the total number of copper atoms. 5.The titrations of the 610-nm absorbance band are interpreted in terms of two non-identical Type I Cu2+ having oxidation-reduction potentials of 490 and 580 mV, respectively, in acetate buffer (pH 5.5). Both Type 1 ions have the same extinction coefficient at 610 nm, 5.5 mM−1·cm−1. Reductive titrations with Fe2+ or ascorbate or oxidative titrations with O2 all produced the same titration curves, which also were independent of mediator concentration in a rather large range. 6.The titration behavior of the 330-nm chromophore was found to be complicated and no simple interpretation directly associating this absorption with the redox state of a one- or two-electron acceptor was found possible." @default.
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- W2018910615 date "1973-06-01" @default.
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- W2018910615 title "The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin" @default.
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- W2018910615 doi "https://doi.org/10.1016/0005-2795(73)90112-8" @default.
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