Metallothionein '96

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منابع مشابه

Anti-metallothionein IgG and levels of metallothionein in autistic families.

Metallothioneins (MTs) are a family of small proteins containing 61-68 amino acids with an unusually high concentration of cysteine. MT-1, the most functional and active MT in humans, has the ability to react with and enhance the detoxification of a number of metals including zinc, mercury, copper and cadmium. MT dysfunction may result, then, in many of the aetiological syndromes observed in au...

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Metallothionein in Brain Disorders

Metallothioneins are a family of proteins which are able to bind metals intracellularly, so their main function is to regulate the cellular metabolism of essential metals. There are 4 major isoforms of MTs (I-IV), three of which have been localized in the central nervous system. MT-I and MT-II have been localized in the spinal cord and brain, mainly in astrocytes, whereas MT-III has been found ...

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Structure of mammalian metallothionein.

All mammalian metallothioneins characterized contain a single polypeptide chain of 61 amino acid residues, among them 20 cysteines providing the ligands for seven metal-binding sites. Native metallothioneins are usually heterogeneous in metal composition, with Zn, Cd, and Cu occurring in varying proportions. However, forms containing only a single metal species, i.e., Zn, Cd, Ni, Co, Hg, Pb, Bi...

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Metallothionein and cancer

2. Roles of metallothionein in the cells The first discovered and still not fully understood roles of MT-1 and MT-2 are transporting of essential heavy metals, detoxification of toxic ones and protection against oxidation stress. MT by interaction with other proteins fulfils its function, resulting in different effects in the organism [5]. Interaction of MT with other proteins occurs either dir...

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The ATP-metallothionein complex.

We have previously shown that glutathione (GSH) and glutathione disulfide interact with metallothionein (MT) and modulate its capacity to donate and transfer zinc. In this paper, we show that ATP also forms a 1:1 complex with MT (Kd = 176 +/- 33 microM, pH 7. 4) that enhances the transfer of zinc to zinc-depleted sorbitol dehydrogenase, increases the rate of thiol-disulfide interchange with Ell...

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ژورنال

عنوان ژورنال: Journal of UOEH

سال: 1997

ISSN: 0387-821X,2187-2864

DOI: 10.7888/juoeh.19.57