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• W2061840699 abstract "Abstract Thyroidal particulate protein with peroxidase activity has been studied to determined wetherr it could be induced to form a sulfenyl iodide, postulated as a reactive intermediate in the iodination of tyrosine. The protein was solubilized with digitonin and purified by tryptic digestion and filtration through Sephadex G-200. When supplemented with H 2 O 2 it catalyzed the oxidation of guaiacol iodide or thiourea at 37°C. With iodide as substrate the product was an iodoprotein. In the absence of H 2 O 2 the protein did not bind 131 I − or thio[ 14 C] urea unless it first had been dialyzed against [ 36 Cl] chlorinated buffer. During dialysis a portion of the 36 Cl from the dialysis medium was bound by protein. Subsequent binding of iodide or thiourea was accompanied by loss of protein-bound 36 Cl. Addition of iodide to dialyzed protein at 4°C resulted in formation of a yellow compound with maximum absorbance at 355 nm. It was postulated to be a sulfenyl periodide on the basis of its absorption spectrum and its behavior with thio[ 14 C] urea and 2-mercaptoethanol. The stability of the colored species was dependent on temperature and concentration of iodide. Disappearance of color as the solution was warmed was accompanied by formation of iodo-protein. Predialysis of the protein against p -chloromercuribenzoate, but not 2-mercaptoethanol or bisulfite, prevented the formation of the yellow proteiniodide species, indicating that a reactive sulfhydryl group was involved in the reaction. It was concluded that a particulate protein closely asscociated with thyroid peroxidase could be induced by non-enzymatic means to form a species which has properties consistent with those of a sulfenyl iodide. Further investigation will be required to determine whether the same protein-iodine species can be identified during the peroxidase-catalyzed oxidation of iodide." @default.
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• W2061840699 date "1974-01-25" @default.
• W2061840699 modified "2023-09-27" @default.
• W2061840699 title "Non-enzymatic formation of sulfenyl iodide by solubilized thyroid particulate protein with peroxidase activity☆" @default.
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• W2061840699 doi "https://doi.org/10.1016/0304-4165(74)90358-4" @default.
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