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Fractionation of enzymatically methylated acid-insoluble proteins from thymus nuclei

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Abstract

Isolated calf thymus nuclei werein 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 radio-activity. 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 0.5 N NaOH contained the largest amount of radioactivity. This protein was found to be basic in nature by amino analysis.

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Authors and Affiliations

  1. College of Pharmacy, Sung Kyun Kwan University, 170, Suwon Kyunggi-do, Korea

    Hyang Woo Lee

  2. Fels Research Institute, Temple University School of Medicine, 19140, Philadelphia, PA, U.S.A.

    Sangduk Kim & Woon Ki Paik

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  1. Hyang Woo Lee
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  2. Sangduk Kim
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  3. Woon Ki Paik
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Lee, H.W., Kim, S. & Paik, W.K. Fractionation of enzymatically methylated acid-insoluble proteins from thymus nuclei. Arch. Pharm. Res. 9, 157–161 (1986). https://doi.org/10.1007/BF02900000

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