USING OF ELECTROCHEMICAL METHODS FOR STUDYING OF METALLOTHIONEIN CONTENT IN THE HUMAN BLOOD SERUM OF A PATIENT POISONED BY LEAD AND TREATED BY PLATINUM

Jitka Petrlová,David Potěšil,René Kizek,Jiří Kukačka,Vojtěch Adam,Radka Mikelová,Richard Průša,Ondřej Blaštík,Josef Zehnálek

doi:10.5507/bp.2005.086

Abstract

Metallothioneins belong to the group of intracellular, high molecular and cysteine-rich proteins whose content increase with increasing concentration of a heavy metal. Here we applied the adsorptive transfer stripping differential pulse voltammetry Brdicka reaction for the determination of metallothionein in human blood serum of patient poisoned by lead and/or treated by platinum. The increased metallothionein concentrations in both cases were observed.

Highlights

Metallothionein (MT) belongs to the group of intracellular, high molecular and cysteine-rich proteins with molecular weight from 6 to 10 kDa
Cysteine sulfhydryl groups participate in covalent bindings with heavy metals
The N-terminal part of the protein is marked as α-domain, which has three binding places for divalent ions. β-Domain (C-terminal part) has the ability to bind four divalent ions of heavy metals

Summary

Introduction

Metallothionein (MT) belongs to the group of intracellular, high molecular and cysteine-rich proteins with molecular weight from 6 to 10 kDa (ref.[1]). The MT was discovered in 1957, when Margoshes and Valee isolated it from horse kidney[2]. MTs consist of two binding domains (α, β) that are assembled from cysteine clusters. Cysteine sulfhydryl groups participate in covalent bindings with heavy metals. The N-terminal part of the protein is marked as α-domain, which has three binding places for divalent ions. Β-Domain (C-terminal part) has the ability to bind four divalent ions of heavy metals. A group of human metallothioneins such as MT1, MT2, MT3 and MT4 has been described (Table 1)

Objectives

Methods

Results