Triton-Gel Electrophoresis of Histones Containing Oxidized Methionine and Cysteine Residues
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概要
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Electrophoresis in polyacrylamide gels in the presence of 6mM Triton X-100 in 0.9M acetic acid and 6.25M urea gave a high resolution of separation of the histones in which methionines and cysteines, respectively, are oxidized to the sulfoxides or sulfones (H2A, H2B, H3, H4) and to form an intramolecular disulfide bond (H3). The methionine-oxidized histones migrated faster than untreated histones. The electrophoretic mobility of histone H3 also increased by oxidation of the two cysteines to a cystine. The increase of the mobilities might be explained in terms of the decrease of the helical contents of the histones by the oxidation of methionine and/or cysteine residues.
- 群馬大学の論文
- 1984-03-30
著者
関連論文
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