Journal ArticleDOI
Iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase.
Ronald P. Magnusson,Alvin Taurog +1 more
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TLDR
The stimulatory effect of iodide could not be explained by protection of the enzymes against inactivation by H2O2, and a mechanism is suggested involving an enzyme-hypoiodite complex as an intermediate.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1983-04-29. It has received 34 citations till now. The article focuses on the topics: Lactoperoxidase & Iodide.read more
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Journal ArticleDOI
Mechanism of iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase.
TL;DR: It is suggested that the latter can react with H2O2 in a catalase-like reaction, with evolution of O2, which is also involved in iodination of tyrosine, oxidation of thioureylene drugs, and oxidation of I-, and that inhibition of catalatic activity by these agents occurs through competition with H 2O2 for oxidized iodine.
Journal ArticleDOI
Mechanisms of thyroid peroxidase- and lactoperoxidase-catalyzed reactions involving iodide.
TL;DR: It is postulated that lactoperoxidase generates hypoiodous acid and that the latter is the active intermediate in the various reactions involving iodide.
Journal ArticleDOI
Duox expression and related H2O2 measurement in mouse thyroid: onset in embryonic development and regulation by TSH in adult.
Milutin Milenkovic,Xavier De Deken,Ling Jin,Mario De Felice,Roberto Di Lauro,Roberto Di Lauro,Jacques Emile Dumont,Bernard Corvilain,Françoise Miot +8 more
TL;DR: The onset of Duox protein expression is compatible with their proposed function in thyroid hormone synthesis and it can be considered as a functional marker of the developing thyroid, however, Duox expression in adult is much less regulated by TSH than NIS and thyroperoxidase.
Journal ArticleDOI
Structure and molecular interactions of anti-thyroid drugs. Part 3.1 Methimazole: a diiodine sponge
TL;DR: Hard and soft acid–base chemistry might explain the two mechanisms of action of anti-thyroid drugs, the inhibition of thyroid peroxidase via coordination to the hard heme group and the trapping of oxidized iodides via complexation of soft iodinated Lewis acids.
Journal ArticleDOI
The Mechanism of Action of Synthetic Antithyroid Drugs: Iodine Complexation During Oxidation of Iodide
TL;DR: The results suggest that synthetic antithyroid agents may act either on peroxidase and/or the molecular iodine which may be produced by oxidation of iodides (2I(-)----I2----2I+).
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Book ChapterDOI
[7] Mitochondrial respiratory control and the polarographic measurement of ADP : O ratios
TL;DR: This chapter discusses the mitochondrial respiratory control and the polarographic measurement of ADP : O ratios and the principle of the oxygen electrode has been summarized, and the design of the vibrating oxygen electrode for use with speetrophotometric studies is illustrated.
Journal ArticleDOI
The cellular production of hydrogen peroxide
TL;DR: The cytochrome c peroxidase assay is suitable for use with subcellular fractions from tissue homogenates as well as with pure enzyme systems to measure H(2)O( 2) generation and can be made on the basis of the rates with the isolated fractions under physiological conditions.
Journal ArticleDOI
Peroxidase-Catalyzed Halogenation
M Morrison,G R Schonbaum +1 more
TL;DR: A proposed mechanism for this reaction suggests that the oxidation is mediated by the iodoenzyme derivative followed by a prototropic rearrangement and scission to form the ether bound of thyronine and a serine residue on thyroglobulin.
Journal ArticleDOI
Chloroperoxidase. VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme.
TL;DR: Results indicate that Compound I of chloroperoxidase may contain a reactive oxygen atom, and by analogy with organic mechanisms for the decomposition of peracids, these results indicate that the enzyme also oxidizes ethanol to form acetaldehyde.