Abstract
The sensor component of bacterial mercury resistance systems is the metalloregulatory protein MerR, which has nanomolar sensitivity and high selectivity for Hg(II). A fusion protein of MerR and the α-peptide part of β-galactosidase (LacZα) was constructed by fusing the relevant genes. The protein exhibited both MerR functions and α-complementing activity to the inactive LacZΔM15 (M15) protein. The bifunctional character of the appropriate MerR–LacZα-complemented M15 protein (MerR–LacZα:M15 protein complex) was used to develop a Hg(II)-specific enzyme-complemented activatorsorbent assay. Hg(II) was immobilized and presented on a matrix taking advantage of the high affinity of Hg(II) to SH residues. The immobilized Hg(II) could be specifically detected down to the parts-per-billion level by quantifying the β-galactosidase activity of the bound fusion protein complex.
Published Version
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