Fractionation of enzymatically methylated acid-insoluble proteins from thymus nuclei

  • Lee, Hyang-Woo (College of Pharmacy, Sung Kyun Kwan University) ;
  • Kim, Sang-Duk (Fels Research Institute, Temple University School of Medicine) ;
  • Paik, Woon-Ki (Fels Research Institute, Temple University School of Medicine)
  • Published : 1986.09.01

Abstract

Isolated calf thymus nuclei were in vitro methylated with S- adenosy-L-methyl-$^{14}C$ methionine, and the proteins were fractionated according to their solubilities. Histone fraction ($H_{2}SO_{4}$-soluble fraction) contained approximately 60% total radioactivity incorporated, while "residual protein" which was ($H_{2}SO_{4}$-insoluble contained the remaining radio-activity. The "residual protein" was further fractionated into various acidic proteins, which contained very littel 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.

Keywords