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  • Author: R. K. Banerjee x
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P. K. De and R. K. Banerjee


A highly active soluble peroxidase has been identified in the preputial glands of the rat. The enzyme was detectable in the sebaceous secretion of the glands and showed catalytic properties characteristic of true peroxidase. It had a native molecular weight of around 73 000 as determined by gel-permeation studies. Immunologically the enzyme cross-reacted with an antiserum against bovine lactoperoxidase. Administration of progesterone resulted in a significant increase in the total activity of the enzyme, while testosterone and oestradiol had no such effect. The enzyme had a similar molecular weight and similar catalytic and immunological properties to rat uterine fluid peroxidase but differed markedly in respect to sensitivity to oestradiol.

J. Endocr. (1987) 112, 239–245

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R. K. Banerjee, A. K. Bose, T. K. Chakraborty, S. K. De and A. G. Datta


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.

J. Endocr. (1985) 106, 159–165