Studies on the Membrane-Associated Nature of Human Thyroid Peroxidase: A Difference in the Solubility of the Enzyme from Benign and Malignant Thyroid Tissues*
Autor: | B Davidson, Morris Soodak, Charles Nakamura, Austin L. Vickery, Farahe Maloof, J T Neary |
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Rok vydání: | 1978 |
Předmět: |
Adenoma
endocrine system medicine.medical_specialty Goiter Chemical Phenomena endocrine system diseases Octoxynol Endocrinology Diabetes and Metabolism Clinical Biochemistry Thyroid Gland Iodide Peroxidase Biochemistry Polyethylene Glycols Thyroid carcinoma Endocrinology Thyroid peroxidase Microsomes Internal medicine medicine Humans Thyroid Neoplasms biology Chemistry Carcinoma Biochemistry (medical) Thyroid Intracellular Membranes medicine.disease medicine.anatomical_structure Peroxidases Solubility Membrane protein biology.protein Microsome Peroxidase |
Zdroj: | The Journal of Clinical Endocrinology & Metabolism. 46:791-799 |
ISSN: | 1945-7197 0021-972X |
DOI: | 10.1210/jcem-46-5-791 |
Popis: | Thyroid peroxidase (TPO) is an integral membrane protein. The intact protein can be solubilized from porcine thyroid 105,000 X g particles (“microsomal” membranes) by Triton X-100 and other nonionic detergents (J Biol Chem 251: 2525, 1976). The Triton X-100 solubilization procedure has now been applied to human thyroid microsomal membranes in an effort to investigate the membrane nature of TPO in thyroid disorders. We studied tissues from 6 patients with thyroid carcinoma (papillary, follicular, and oxyphilic cell), 10 with adenoma (macrofollicular, follicular, microfollicular, and trabecular), 1 with multinodular nontoxic goiter, and 6 with diffuse toxic goiters. Normal tissue was obtained from 4 of the carcinoma patients and 8 of the adenoma patients. TPO activity in thyroid homogenates was determined by the guaiacol assay method. icrosomes from each homogenate were prepared by centrifugation of the 8500 x g supernatant at 105,000 X g for 1 h, and the microsomes were washed hypotonically to release entr... |
Databáze: | OpenAIRE |
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