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Titlebook: Metallothionein IV; Curtis D. Klaassen Book 1999 Springer Basel AG 1999 DNA.apoptosis.autoimmune disease.cell culture.gene expression.kidn

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楼主: CHARY
发表于 2025-3-26 21:29:25 | 显示全部楼层
Nomenclature of metallothionein: Proposal for a revision that time, a large number of additional amino acid sequences of metallothionein have become known yielding ample phylogenetic information. On the basis of this development, a new revision of the nomenclature is proposed.
发表于 2025-3-27 01:49:29 | 显示全部楼层
Metallothionein: Molecular evolution and classification[2]. According to this convention class I includes all proteinaceous MTs with locations of Cys closely related to those in the mammalian forms. Class II comprises proteinaceous MTs which lack this property. Class III subsumes metallopolyisopeptides containing gammaglutamyl-cysteinyl units resembling in their features proteinaceous MTs.
发表于 2025-3-27 08:43:20 | 显示全部楼层
Quantification of cytosolic metallothionein contents by a developed assay system using immobilized aoteins are not fully understood, it is believed to play an important role in the homeostasis of essential heavy metals such as Zn and Cu, as well as the detoxification of heavy metals such as Cd and Hg [2]. The biosynthesis of MT can be induced by a variety of physical, chemical, sensory and psychological stressors [2–5].
发表于 2025-3-27 13:30:39 | 显示全部楼层
Protein engineering of metallothionein to study the metal-binding abilityIt is well known that metals play an important role in post-transcriptional modifications of proteins stabilizing their structure and physiological activity [1]. The mechanism by which biosynthesized proteins interact with metals and originate such cluster structures like metallothionein (MT) remain unclear.
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Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its α- and β-domain-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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The growth inhibitory activity of metallothionein-3 correlates with its novel β domain sequence rathX-XCys motifs. The GIF gene also has a similar intron/exon structure to that of mammalian MT-1 and MT-2 leading to its classification as MT-3 [2]. Relative to mammalian MTs, MT-3 contains two inserts, a single threonine residue in the N-terminal β-domain and a glutamine rich hexapeptide in the C-terminal α-domain.
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