Thyroid Hormone Residues Are Released from Thyroglobulin with Only Limited Alteration of the Thyroglobulin Structure
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چکیده
منابع مشابه
Thyroid Hormone Synthesis in Thyroglobulin
~-14C]Tyrosine-labeled noniodinated hog thyroglobulin was iodinated enzymatically and nonenzymatically (iodine, iodide-chloramine-T, pH 7.4, or iodine monochloride, p.H 8.1). This led to similar levels of iodine incorporatzon as well as of thyroid hormone synthesis. Iodine monochloride at pH 5.5 formed “hormonogenic” iodotyrosine residues, but no hormone residues. The latter were formed when th...
متن کاملIdentification of thyroid hormone residues on serum thyroglobulin: a clue to the source of circulating thyroglobulin in thyroid diseases.
Thyroglobulin (Tg) present in the serum of normal individuals and patients with thyroid disorders could be partly newly synthesized non-iodinated Tg and partly Tg containing iodine and hormone residues originating from the lumen of thyroid follicles. With the aim of examining the contribution of the latter source of Tg to the elevation of serum Tg concentration in thyroid pathophysiological sit...
متن کاملProduction of anti-human thyroglobulin and anti-thyroid hormone antibodies in rabbits immunized with human thyroglobulin.
Two rabbits (TG-1, TG-2) were immunized with human thyroglobulin (HTg) and bled serially. Antisera were obtained at different times after the first immunization and kept separately and studied. In both rabbits production of anti-HTg, and anti-thyroid hormone antibodies such as anti-thyroxine (T4) and anti-triiodothyronine (T3) antibodies was observed. Binding parameters of anti-HTg antibodies w...
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متن کاملThyroglobulin interactions with thyroid membranes. Relationship between receptor recognition of N-acetylglucosamine residues and the iodine content of thyroglobulin preparations.
Bovine thyroglobulin has been subjected to sequential glycohydrolase treatment in order to define further the components of the carbohydrate chain which are important in binding of the glycoprotein to bovine thyroid membranes. Preparations of asialoagalactothyroglobulin exhibit the best binding, suggesting that exposed N-acetylglucosamine residues on the B carbohydrate chain of thyroglobulin pl...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63901-8