Purified rat liver NADPH-cytochrome c reductase supports iodination of tyrosine in a system including NADPH, cytochrome c and thyroid peroxidase. Catalase inhibits the iodination of tyrosine, while superoxide dismutase has no effect. Antibody developed in the rabbit against purified rat liver NADPH-cytochrome c reductase inhibits both reduction of cytochrome c and tyrosine iodination supported by the enzyme. The antibody forms a single precipitation line with thyroid extract, and inhibits NADPH cytochrome c reductase activity of the thyroid. The antibody partially inhibits iodination in a thyroid mitochondrialmicrosomal fraction, but does not inhibit NADHdependent iodination. The immunochemical studies indicate the participation of NADPHcytochrome c reductase in thyroidal H2O2 generation, and the independent existence of NADPHdependent and NADH-dependent H2O2 generation mechanisms in the thyroid. (Endocrinology96: 1022, 1975)

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