Hydrogen Ion Equilibria of Interaction of Ribonucleic Acid and Albumin-Bovine

Abstract

On interaction of ribonucleic acid and albumine-bovine the
hydrogen ion equilibrium is altered both in aqueous and in 0.25 M
KC1 solution. The ± interaction in the protein chain makes the
alteration in pH more prominent in salt solution than in aqueous
medium. In acid titration this feature is absent Conformational
changes are also accompanied with the availabilities of charged sites
in the interacting species of the protein and nucleic acid. A structural
variation is expected to modulate the translation of conserved RNA
in the protein synthesis during the interaction.