Efficient thyroid hormone formation by in vitro iodination of a segment of rat thyroglobulin fused to Staphylococcal protein A.

Abstract

A polypeptide of 224 amino acids from the C terminus of rat thyroglobulin fused to Staphylococcal protein A (TgC 224), containing 3 tyrosines which have been shown to be hormonogenic in vivo (Tyr-2555, -2569 and -2748), forms thyroid hormones with relatively high efficiency upon in vitro enzymatic iodination using, most likely, the hormonogenic Tyr-2555 and Tyr-2569. Acetylcholinesterase, which has sequence and structural homology with the C terminus of the thyroglobulin molecule and bovine serum albumin, used as control proteins, formed thyroid hormones with lower efficiency. These results validate our experimental approach to define the structural requirements for thyroid hormone formation using thyroglobulin fragments.

Cite this paper

@article{Asuncin1992EfficientTH, title={Efficient thyroid hormone formation by in vitro iodination of a segment of rat thyroglobulin fused to Staphylococcal protein A.}, author={Mar{\'i}a Asunci{\'o}n and Rosaria Ingrassia and Julio Escribano and Ulrich Martin and Ernesto M{\'e}ndez and Roberto Di Lauro and Leonor Lamas}, journal={FEBS letters}, year={1992}, volume={297 3}, pages={266-70} }