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Banerjee
Endocrine control of extrathyroidal peroxidases and iodide metabolism.
De SK, Ganguly CK, Chakraborty TK, Bose AK, Banerjee RK.
Acta Endocrinol (Copenh). 1985 Nov;110(3):383-7.
[abstract only]
"The role of the thyroid and adrenal glands on iodide transport and peroxidase-catalyzed formation of iodotyrosines in extrathyroidal tissues such as stomach and submaxillary glands has been investigated. Thyroidectomy stimulates iodide concentration and iodotyrosine formation in stomach, sensitive to the administration of thyroxine but having no effect on the peroxidase activity. In contrast, although thyroidectomy stimulates the submaxillary peroxidase which is reversed on treatment with thyroxine, it has no effect on iodide concentration and organification in the submaxillary gland. Gastric peroxidase activity is specifically stimulated by adrenalectomy and is inhibited by glucocorticoids which also inhibit iodotyrosine formation in stomach."
Peroxidase-catalysed iodotyrosine formation in dispersed cells of mouse extrathyroidal tissues.
Banerjee RK, Bose AK, Chakraborty TK, De SK, Datta AG.
J Endocrinol. 1985 Aug;106(2):159-65.
[abstract only]
"A method has been developed for the isolation of cells, high in iodine uptake and peroxidase activity, from the stomach and submaxillary gland of mice. The isolated cells could produce protein-bound monoiodotyrosine, di-iodotyrosine and an unknown iodocompound. The reactions were catalysed by peroxidase and were sensitive to antithyroid drugs and haemoprotein inhibitors but were insensitive to TSH. In-vitro iodination of stomach or submaxillary soluble proteins with the respective peroxidase yielded similar iodocompounds while thyroxine was produced when thyroglobulin was used instead."
Iodide carrier in isolated cells of stomach.
Banerjee RK, Bose AK, Chakravartty TK, De SK, Datta AG.
Indian J Biochem Biophys. 1985 Feb;22(1):36-7.
[citation only]
Gastric peroxidase--localization, catalytic properties and possible role in extrathyroidal thyroid hormone formation.
Banerjee RK, Datta AG.
Acta Endocrinol (Copenh). 1981 Feb;96(2):208-14.
[abstract only]
"A highly active peroxidase (EC 1.11.1.7) has been found to be localized in the mitochondria isolated from the fundic region of mouse stomach. The stomach has also the property of concentrating iodide significantly. Evidence has been presented to show that the peroxidase is orientated outside the mitochondrial membrane. The enzyme is strongly inhibited by antithyroid drugs like methimazole and thiouracil. Azide and cyanide completely inactivate the enzyme. The activity is inhibited by SH-blocking reagents like mersalyl or p-chloromercuribenzene sulphonate, but not by N-ethyl-maleimide. The enzyme is also sensitive to the action of some proteolytic enzymes. It can catalyse the formation of mono- or diiodotyrosine from tyrosine or monoiodotyrosine as substrate, respectively. The enzyme is capable of synthesizing thyroxine and triiodothyronine on the backbone of a protein, such as thyroglobulin or albumin."
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