Iodination and oxidation of thyroglobulin catalyzed by thyroid peroxidase.
作者： M Nakamura , I Yamazaki , H Nakagawa , S Ohtaki , N Ui
DOI: 10.1016/S0021-9258(17)43667-2
关键词:
摘要: The kinetics of iodination and oxidation hog thyroglobulin were studied with purified thyroid peroxidase the results compared reactions free tyrosine. From Lineweaver-Burk plots on basis a value 0.83 for delta epsilon mM at 289 nm/iodine atom incorporated, rate constant transfer an assumed enzyme-bound iodinium cation to was estimated be 6.7 X 10(7) 2.3 M-1 s-1 in native (iodine content = 1.0%) more iodinated 1.2%) thyroglobulins, respectively. This iodine-transferring reaction stimulated by iodothyronines, similarly as observed inhibited GSH, inhibition being competitive thyroglobulin. Thyroglobulin oxidized presence system without giving any appreciable change absorbance around 300 nm. stopped flow data, concluded occur way two-electron Compound I 1.0 s-1. kinetic pattern similar that tyrosine monoiodotyrosine. About 6 mol hydrogen peroxide consumed per Thyroid catalyzed thyroglobulin-mediated but lactoperoxidase did not.
sci-hub.st 参考文章(43)
ALVIN TAUROG, Thyroid peroxidase and thyroxine biosynthesis. Recent Progress in Hormone Research. ,vol. 26, pp. 189- 247 ,(1970) , 10.1016/B978-0-12-571126-5.50009-1
Harold Edelhoch, The Properties of Thyroglobulin: VIII. THE IODINATION OF THYROGLOBULIN Journal of Biological Chemistry. ,vol. 237, pp. 2778- 2787 ,(1960) , 10.1016/S0021-9258(18)60228-5
J.T. Dunn, A.D. Dunn, D.G. Heppner, P.S. Kim, A discrete thyroxine-rich iodopeptide of 20,000 daltons from rabbit thyroglobulin. Journal of Biological Chemistry. ,vol. 256, pp. 942- 947 ,(1981) , 10.1016/S0021-9258(19)70070-2
J M Gavaret, D Dème, J Nunez, G Salvatore, Sequential reactivity of tyrosyl residues of thyroglobulin upon iodination catalyzed by thyroid peroxidase. Journal of Biological Chemistry. ,vol. 252, pp. 3281- 3285 ,(1977) , 10.1016/S0021-9258(17)40385-1
Toichiro Hosoya, The Role of Thyroid Peroxidase in teh Synthesis of Thyroxine Residues in Thyroglobulin Gunma symposia on endocrinology. ,vol. 5, pp. 219- 230 ,(1968)
S. Ohtaki, H. Nakagawa, S. Kimura, I. Yamazaki, Analyses of catalytic intermediates of hog thyroid peroxidase during its iodinating reaction. Journal of Biological Chemistry. ,vol. 256, pp. 805- 810 ,(1981) , 10.1016/S0021-9258(19)70048-9
S Ohtaki, H Nakagawa, M Nakamura, I Yamazaki, One- and two-electron oxidations of tyrosine, monoiodotyrosine, and diiodotyrosine catalyzed by hog thyroid peroxidase. Journal of Biological Chemistry. ,vol. 257, pp. 13398- 13403 ,(1982) , 10.1016/S0021-9258(18)33462-8
S.B. Chernoff, A.B. Rawitch, Thyroglobulin structure-function. Isolation and characterization of a thyroxine-containing polypeptide from bovine thyroglobulin. Journal of Biological Chemistry. ,vol. 256, pp. 9425- 9430 ,(1981) , 10.1016/S0021-9258(19)68778-8
Luis Lamas, Alvin Taurog, Gaetano Salvatore, Harold Edelhoch, Preferential Synthesis of Thyroxine from Early Iodinated Tyrosyl Residues in Thyroglobulin Journal of Biological Chemistry. ,vol. 249, pp. 2732- 2737 ,(1974) , 10.1016/S0021-9258(19)42690-2
A. van Zyl, Harold Edelhoch, The Properties of Thyroglobulin Journal of Biological Chemistry. ,vol. 242, pp. 2423- 2427 ,(1967) , 10.1016/S0021-9258(18)95978-8