Biopolym. Cell. 1989; 5(5):44-48.
Structure and Function of Biopolymers
Studies of DNA interaction with protein contaminants
1Akhrem A. A., 1Egorova V. P., 2Egorov A. S., 3Krot V. I., 1Lando D. Yu., 1Luka Z. A.
  1. Institute of Bioorganic Chemistry, Academy of Sciences of the Byelorussian SSR
    Minsk, USSR
  2. Institute of Physiology, Academy of Sciences of the Byelorussian SSR
    Minsk, USSR
  3. Lenin Byelorussian State University
    Minsk, USSR
  4. Institute of Photobiology, Academy of Sciences of the Byelorussian SSR
    Minsk, USSR


DNA isolated from the bovine spleen has been investigated for its interaction with protein contaminants. It is shown that the contaminants are not histones and their binding is determined by the nonionic contacts which are destroyed in the presence of urea and retain with high concentrations of NaCl. The protein contaminants do not change thermostability of DNA and they are distributed irregularly among the macromolecules: less than 10 % of DNA contains more than 70 % of all the proteins.


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