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Analytical Sciences
Vol. 19 (2003) No. 12 P 1569-1573



Original Papers

The recombinant human thyroid hormone receptor (TR) was expressed as an in-frame fusion with ten consecutive histidine residues using a bacterial system; then the receptor was immobilized on an Au-electrode with Ni(II)-mediated chemisorption using the histidine tag and thiol-modified nitrilotriacetic acid. The receptor-modified electrode could rapidly detect ligand binding to hTR without any separation procedures, and showed a good response in a concentration-dependent manner. The sensitivity of this biosensor based on ligand-receptor interactions was comparable to those of conventional competitive ligand binding assays using radio-labeled ligands. Our results strongly suggest that our new biosensor can be applied to the identification of new ligands for hTR.

Copyright © 2003 by The Japan Society for Analytical Chemistry

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