Biopolym. Cell. 1989; 5(5):44-48.
Structure and Function of Biopolymers
Studies of DNA interaction with protein contaminants
- Institute of Bioorganic Chemistry, Academy of Sciences of the Byelorussian SSR
Minsk, USSR - Institute of Physiology, Academy of Sciences of the Byelorussian SSR
Minsk, USSR - Lenin Byelorussian State University
Minsk, USSR - Institute of Photobiology, Academy of Sciences of the Byelorussian SSR
Minsk, USSR
Abstract
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.
Full text: (PDF, in Russian)
References
[1]
Davis RW, Simon M, Davidson N. Electron microscope heteroduplex methods for mapping regions of base sequence homology in nucleic acids. Methods Enzymol. 1971;413-28.
[2]
Thomas JO, Kornberg RD. An octamer of histones in chromatin and free in solution. Proc Natl Acad Sci U S A. 1975;72(7):2626-30.
[3]
Fikhman BA. Light diffusion of bacterial suspensions in the visible field of the spectrum. Biofizika. 1963;8:380-4.
[4]
Yevdokimov YuM, Skuridin SG, Akimenko NM. Low molecular weight liquid crystalline microPhases double-stranded nucleic acids and synthetic Polynucleotides. Vysokomolekulyarnye Soedineniya. 1984; 26(11):2403-10.
[5]
Lowry OH, Rosebrough NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193(1):265-75.
[6]
Slonim IYa. Particle size determination by light scattering. Optics and spectroscopy. 1970; 8(1):98-108.