Summary
Heterologous expression in E.coli, coupled with spectroscopic analyses, has enabled the metal binding properties of the recombinant mouse Zn-MT, Zn-αMT and Zn-βMT to be characterized. Cd(II) binding properties of Zn7-MT and Zn4-αMT have shown that they behave like the native proteins and those of the Zn3-βMT fragment have been reported for the first time. In contrast, the behavior of these proteins towards Hg(II), Cu(I) and Ag(I), which is strongly influenced by the pH and the stabilization time, differs from that of the native forms. Furthermore, recombinant Cd-βMT has also been expressed and characterized.
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Atrian, S. et al. (1999). Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its α- and β-domains. In: Klaassen, C.D. (eds) Metallothionein IV. Advances in Life Sciences. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8847-9_8
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DOI: https://doi.org/10.1007/978-3-0348-8847-9_8
Publisher Name: Birkhäuser, Basel
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