19 octobre 2012

Metal binding of Metallothionein

Metallothionein has been documented to bind a wide range of metals including cadmium, zinc, mercury, copper, arsenic, silver, etc. Metallation of MT was previously reported to occur cooperatively but recent reports have provided strong evidence that metal-binding occurs via a sequential, noncooperative mechanism. The observation of partially metallated MT (that is, having some free metal binding capacity) suggest that these species are biologically important.Metallothioneins likely participate in the uptake, transport, and regulation... [Lire la suite]
Posté par tnfalpha à 09:36 - Commentaires [0] - Permalien [#]

19 octobre 2012

Structure and classification of Metallothionein

Metallothioneins are present in a vast range of taxonomic groups, ranging from prokaryotes (such as the cyanobacteria Syneccococus spp....), protozoa (p. ex. the ciliate Tetrahymena genera...), plants (such as Pisum sativum, Triticum durum, Zea mays, Quercus suber...), yeast (such as Saccharomyces cerevisiae, Candida albicans,...), invertebrates (such as the nematode Caenorhabditis elegans, the insect Drosophila melanogaster, the mollusc Mytilus edulis, or the echinoderm Strongylocentrotus purpuratus) and vertebrates (such as the... [Lire la suite]
Posté par tnfalpha à 09:35 - Commentaires [0] - Permalien [#]
19 octobre 2012

Metallothionein

Metallothionein (MT) is a family of cysteine-rich, low molecular weight (MW ranging from 500 to 14000 Da) proteins. They are localized to the membrane of the Golgi apparatus. MTs have the capacity to bind both physiological (such as zinc, copper, selenium) and xenobiotic (such as cadmium, mercury, silver, arsenic) heavy metals through the thiol group of its cysteine residues, which represents nearly the 30% of its amino acidic residues.MT was discovered in 1957 by Vallee and Margoshe from purification of a Cd-binding protein from... [Lire la suite]
Posté par tnfalpha à 09:35 - Commentaires [0] - Permalien [#]