Studies on the structure of ribosomal ribonucleic acid from normal and tumour tissues.

Abstract

The dissociation properties of ribosomal RNA from liver and hepatoma were found to be dependent upon the temperature, ionic strength and cationic valency of the solvent. On increasing the temperature the pK values of the Ν1 H— C6=O and N1 = C6 — NH2 groups of nucleobases were displaced towards neutrality due to the thermal cleavage of Η-bridge linkages. Consequently, as the temperature is increased the nucleic acids bind increasingly more equivalents of acid or alkali. On forward- and back-titration hysteresis is observed in the acid pH range and the degree of hysteresis is found to decrease as the temperature is increased. Increasing the ionic strength of monovalent cations from μ=0.005 to 0.05 Na® leads to a reduced binding of equivalents of acid and alkali brought about by the displacement of pK values towards more extreme pH-values and to an increase in the stability of secondary structure. Bivalent cations exert a stronger stabilizing effect on the molecular conformation of nucleic acids than monovalent cations of equal ionic strength. The more pronounced displacement of the PK values of ionizable groups on titration from pH 7 to pH 3 may be attributed to the additional action of bivalent cations as chelate formers. Significant differences in the acid-base properties of ribosomal RNA from liver and hepatoma were observed especially at low temperatures and high ionic strength. At 5 °C and μ=0.1 NaCl less equivalents of acid and alkali are bound by hepatoma RNA than by liver RNA due to a lower degree of dissociation particularly of the N1=C6—NH2, and Ν1H — C6=0 groups.