Interaction of basic oligo-L-amino acids with deoxyribonucleic acids. Oligo-L-arginines of various chain lengths and herring sperm DNA.
The interaction of DNA and oligo-L-arginines having definite chain lengths of 1-17 residues was studied by precipitate formation and thermal denaturation of the complexes in order to obtain a better understanding of the roles of nuclear basic proteins. The results can be summarized as follows. 1. Those oligo-L-arginines, (Arg)n, in which n greater than or larger than 4 can bind with DNA irreversibly to form precipitates of the complexes. Among them, oligomers larger than (Arg)5 precipitate DNA completely in Arg/P input ratios below 1. The Arg/P ratios in the precipitates are between 0.6-0.8. 2. The thermal stability of the complexes depends on the method of complex formation, and complexes formed by the dialysis method are more stable than those formed by the mixing method. 3. The binding of (Arg)n to DNA was found to be reversible and in a equilibrium for n less than or equal to 6. In general, the longer the oligomer, the higher the stability of the complex at a definite Arg/P ratio. 4. For (Arg)7-10, three kinds of complexes with different stabilities are formed between DNA and oligopeptides. 5. For (Arg)14-17, only a restricted type of complexes can be formed between DNA and oligomers, as in the case with poly-L-arginine or protamines. 6. The interaction between basic nuclear proteins and DNA is discussed in the light of the basic region in protamine and histone molecules.
D000818:Animals; D001120:Arginine; D055598:Chemical Phenomena; D002621:Chemistry; D004247:DNA; D004355:Drug Stability; D005399:Fishes; D006358:Hot Temperature; D008297:Male; D009691:Nucleic Acid Denaturation; D009698:Nucleoproteins; D009842:Oligopeptides; D010455:Peptides; D011489:Protein Denaturation; D013094:Spermatozoa
D009698:Nucleoproteins; D009842:Oligopeptides; D010455:Peptides; D004247:DNA; D001120:Arginine