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KUNIHIRO YAMAMOTO, LESLIE J. DEGROOT, Participation of NADPH-Cytochrome C Reductase in Thyroid Hormone Biosynthesis, Endocrinology, Volume 96, Issue 4, 1 April 1975, Pages 1022–1029, https://doi.org/10.1210/endo-96-4-1022
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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)