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Pregled bibliografske jedinice broj: 2635

Cadmium binding to metallothioneins

Erk, Marijana; Raspor, Biserka
Cadmium binding to metallothioneins // 6. EMINar / Bakran-Petricioli, Tatjana (ur.).
Zagreb: Eurocoast-hrvatska udruga, 1997. str. 33-33 (poster, nije recenziran, sažetak, znanstveni)

Cadmium binding to metallothioneins

Erk, Marijana ; Raspor, Biserka

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

6. EMINar / Bakran-Petricioli, Tatjana - Zagreb : Eurocoast-hrvatska udruga, 1997, 33-33

6. godišnji skup European Marine Interdisciplinary Network

Mjesto i datum
Sali, Hrvatska, 02-06.04.1997

Vrsta sudjelovanja

Vrsta recenzije
Nije recenziran

Ključne riječi
Cadmium binding to metallothioneins
(Kompleksno vezanje kadmija na metalotionein)

Metallotioneins (MTs) are small, metal-binding proteins that are rich on cysteine residues. SH-groups are involved in the metal coordination that is considered essential to the structure and the function of the protein. MTs can be induced by and bind essential metals copper and zinc and toxic metals such as cadmium, mercury and silver, and are widely distributed in both vertebrate and invertebrate species. In environmental studies bivalves of the genus Mytilus are used as indicator organisms for monitoring the pollution of the coastal seawater with heavy metals.1 The mussel MT exhibits more similarity to vertebrate MTs than to those of non-molluscan invertebrates. Isoforms of mussel MTs exhibit homology to mammalian class I MTs. A voltammetric study on the binding properties of the rabbit liver metallothionein (fractions I and II) Sigma M 7641 for cadmium ions was performed. The capacity of MT to complex cadmium and the stability constants of Cd-MT complex have been determined from the direct titration of MT with cadmium ions in 0.59 M sodium cloride medium at pH 7.9 and 2.0. At pH 7.9 the formation of the Cd-MT complex has been followed measuring the specific anodic signal height of the complex.2 Stability constants of Cd-MT have been evaluated from the experimental data using different procedures.3 The results will be discussed and the reliable evaluation procedure proposed. 1. Roesijadi, G. (1996). Metallothionein and its role in toxic metal regulation. Comp. Biochem. Physiol., 113C, 117-123. 2. Raspor, B. & Pavi~i}, J. (1996). Electrochemical methods for quantification and characterization of metallothioneins induced in Mytilus galloprovincialis. Fresenius J. Anal. Chem., 354, 529-534. 3. Raspor, B. & Pavi~i}, J. Electrochemical characterization of metal-binding properties of metallothioneins isolated from Mytilus galloprovincialis. Croat. Chim. Acta, in press.

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Projekt / tema

Institut "Ruđer Bošković", Zagreb