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- W2040983315 abstract "In order to investigate the role of the α-fragment of metallothionein (MT) in metalbinding, two mutant MTs, βAlaαCys- and αCysβCys-mutant MTs, expressed in Escherichia coli were analyzed for their metal-binding ability. A mutant MT where all of the cysteine residues in the β-fragment of MT were substituted by alanine residues and another mutant MT that had the inverse fragment composition (α-β, i. e., β-α in wild-type MT) were designated as the βAlaαCys and the αCysβCys-mutant MT's, respectively. Both expressed Cd-binding mutant MTs were identified by amino acid analyses. From their metal-binding capacities, the two mutant MTs exhibited higher Cd-binding abilities than wild-type MT. The results suggested that the α-fragment plays a key role in the Cd-binding of MT, and that the metal-binding tightness of MT is dependent on the metal- binding ability of a prior fragment in MT." @default.
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- W2040983315 date "1997-01-01" @default.
- W2040983315 modified "2023-09-27" @default.
- W2040983315 title "A mutant metallothionein which has inverse fragment composition exhibits high cadmium-binding ability" @default.
- W2040983315 doi "https://doi.org/10.1080/15216549700201051" @default.
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