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Analysis of interaction between cadmium and metallothionein isoforms by capillary zone electrophoresis
Author(s) -
Minami Takeshi,
Matsubara Hideki,
Ohigashi Masayuki,
Kubo Kanenobu,
Okabe Nobuo,
Okazaki Yuko
Publication year - 1996
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150171019
Subject(s) - cadmium , metallothionein , egta , chemistry , gene isoform , zinc , capillary electrophoresis , chromatography , ether , gel electrophoresis , metalloprotein , ethylene glycol , electrophoresis , polyacrylamide gel electrophoresis , sodium , biochemistry , calcium , enzyme , organic chemistry , gene
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 commericial standard MT‐1 isoform prepared from rabbit liver, the peak area 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 glycol‐bis‐(β‐aminoethyl ether)‐ N , N , N ′ N ′‐tetraacetic acid (EGTA) was added to a solution containing cadmium and MT‐1, the peak area recovered with incrasing 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 change the charge of MT, which may account for the observed differences in electrophoretic behavior.