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The kinetics of the catalysis of Fe(II) oxidation by crystalline human ferroxidase (ceruloplasmin) has been studied under various conditions at 30°. Two Km values with respect to Fe(II), Km1 = 0.6 µm and Km2 = 50 µm, were obtained at pH 6.5, at which ferroxidase gave the maximum activity of 550 Fe(II) per ferroxidase per min in an acetate buffer. Competition between the two substrates, p-phenylenediamine and Fe(II), was observed. The stoichiometry of Fe(II), ferroxidase, and oxygen, determined from the experimental data, was 4:1:1.
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Shigemasa Osaki (1966) studied this question.
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