Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its alpha- and beta-domains

S ATRIAN; R BOFILL; M CAPDEVILA; N COLS; P GONZALEZ-DUARTE; R GONZALEZ-DUARTE; A LEIVA; O PALACIOS; N ROMERO-ISART

doi:10.1007/978-3-0348-8847-9_8

Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its alpha- and beta-domains

S ATRIAN, R BOFILL, M CAPDEVILA, N COLS, P GONZALEZ-DUARTE, R GONZALEZ-DUARTE, A LEIVA, O PALACIOS, N ROMERO-ISART

Departament de Química

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Resum

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

Idioma original	Anglès
Nombre de pàgines	12
ISBN (electrònic)	978-3-0348-8847-9
DOIs	https://doi.org/10.1007/978-3-0348-8847-9_8
Estat de la publicació	Publicada - 1999

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10.1007/978-3-0348-8847-9_8

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title = "Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its alpha- and beta-domains",

abstract = "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",

author = "S ATRIAN and R BOFILL and M CAPDEVILA and N COLS and P GONZALEZ-DUARTE and R GONZALEZ-DUARTE and A LEIVA and O PALACIOS and N ROMERO-ISART",

year = "1999",

doi = "10.1007/978-3-0348-8847-9\_8",

language = "English",

isbn = "978-3-0348-9799-0",

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TY - GEN

T1 - Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its alpha- and beta-domains

AU - ATRIAN, S

AU - BOFILL, R

AU - CAPDEVILA, M

AU - COLS, N

AU - GONZALEZ-DUARTE, P

AU - GONZALEZ-DUARTE, R

AU - LEIVA, A

AU - PALACIOS, O

AU - ROMERO-ISART, N

PY - 1999

Y1 - 1999

N2 - 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

AB - 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

UR - https://link-springer-com.are.uab.cat/chapter/10.1007/978-3-0348-8847-9_8

U2 - 10.1007/978-3-0348-8847-9_8

DO - 10.1007/978-3-0348-8847-9_8

M3 - Other contribution

SN - 978-3-0348-9799-0

ER -

Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its alpha- and beta-domains

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