Abstract
FRIDOVITCH1 identified myoglobin as a contaminant in partially purified preparations of cytochrome c and found the protein moiety of myoglobin to be a potent, competitive inhibitor of cytochrome c reduction by xanthine oxidase. Since the myoglobin of pig and horse heart exhibited markedly different affinity constants for the enzyme, the inhibition seemed to be highly specific for the globin structure1.
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QUINN, J., PEARSON, A. Multiple Bovine Myoglobin Inhibition of Cytochrome c Reduction by Xanthine Oxidase. Nature 201, 928–929 (1964). https://doi.org/10.1038/201928a0
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DOI: https://doi.org/10.1038/201928a0
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