Analysis of interaction between cadmium and metallothionein isoforms by capillary zone electrophoresis

Electrophoresis
T MinamiY Okazaki

Abstract

The effects of cadmium on the peak area of metallothionein (MT) protein were studied by capillary zone electrophoresis with a polyacrylamide-coated tube at neutral pH. When cadmium was added to a commercial standard MT-1 isoform prepared from rabbit liver, the peak are of the MT-1 isoform decreased in a time- and dose-dependent manner. The MT-2 isoform also decreased with time, but the rate of decrease was lower than that of the MT-1 isoform. When ethylene glyco-bis-(beta-aminoethyl ether)-N,N,N'N'-tetraacetic acid (EGTA) was added to a solution containing cadmium and MT-1, the peak area recovered with increasing concentration of EGTA. Zinc caused a slight decrease in the peak areas of MT-1 and MT-2 compared with cadmium, while addition of sodium did not decrease the areas. Furthermore, the peak areas of MT isoforms of the crude extract prepared from zinc-treated mice also decreased with increasing concentration of cadmium. These results indicate that cadmium may changed the charge of MT, which may account for the observed differences in electrophoretic behavior.

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Citations

Jul 13, 2000·Journal of Chromatography. B, Biomedical Sciences and Applications·K KuboT Minami
Feb 17, 2000·Journal of Chromatography. B, Biomedical Sciences and Applications·K KuboT Minami
Oct 4, 2002·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Takeshi MinamiSeiji Ichida
Nov 27, 2002·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Takeshi MinamiKanenobu Kubo
Nov 1, 2011·Journal of Chromatography. a·Marketa RyvolovaRene Kizek
Dec 5, 2009·Electrophoresis·Sona KrizkovaRene Kizek

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