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Effects of aroclor 1254 on proteins of mouse liver: Application of two‐dimensional electrophoretic protein mapping
Author(s) -
Leigh Anderson N.,
Swanson Mark,
Giere Frederic A.,
Tollaksen Sandra,
Gemmell Anne,
Nance Sharron,
Anderson Norman G.
Publication year - 1986
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.1150070106
Subject(s) - xenobiotic , heat shock protein , quantitative analysis (chemistry) , chemistry , microsome , cytochrome , electrophoresis , in vivo , cytochrome p450 , biochemistry , biology , chromatography , metabolism , in vitro , enzyme , genetics , gene
Liver proteins of male C57BL/6T mice treated with 0, 50, or 250 mg/kg Aroclor 1254 were analyzed by high‐resolution two‐dimensional (2‐D) electrophoresis. The resulting patterns were processed using a computerized image analysis system and quantitative data selected for a total of 150 protein spots. On the basis of an analysis of liver proteins form five animals in each treatment group, we found 31 proteins that showed quantitative differences attributable to treatment with chlorinated hydrocarbons at a high level of statistical significance. One of the altered proteins appears to be Mitcon:2, a heat‐shock sensitive mitochondrial matrix polypeptide; another appears likely to be microsomal cytochrome b 5 . The results indicate that quantitative 2‐D protein mapping may reveal much more detail regarding the in vivo effects of toxic xenobiotics than has previously been available, and thus allow a more informative approach to the testing of toxic compounds.