KMID : 0043319860090030157
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Archives of Pharmacal Research 1986 Volume.9 No. 3 p.157 ~ p.161
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Fractionation of Enzymatically Methylated Acid-Insoluble Proteins from Thymus Nuclei
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Lee HW
Kim SD/Paik WK
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Abstract
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Isolated calf thymus nuclei were in vitro methylated with S-adenosyl-L-methyl -14C methionine, and the proteins were fractionated according to their solubilities. Histone fraction(H2SO4-soluble fraction) contained approximately 60% total radioactivity incorporated, while "residual protein" which was H2SO4-insoluble contained the remaining radioactivity. The "residual protein" was further fractionated into various acidic proteins, which contained very little of the radioactivity. However, the protein fraction eluted from DEAE-cellulose with 0.5N NaOH contained the largest amount of radioactivity. This protein was found to be basic in nature by amino analysis.
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