Apparent thermal destabilization of Escherichia coli nucleoprotein due to the incomplete dialysis of EDTA.
Escherichia coli nucleoprotein has been found to undergo thermal denaturation approx. 5 degrees C lower than purified E. coli DNA, measured in 0.25 mM sodium EDTA, pH 8.0 (Searcy, D.G. (1975) Biochim. Biophys. Acta 395, 535-547). This is now shown to be an artifact due to the impermeability of dialysis membranes to sodium EDTA, especially at low concentrations such as 1 mM or less. Thermal denaturation data can be corrected by measuring the electrical conductivity of the solutions. When this is done, the nucleoprotein and DNA both denature at the same temperature.
D001665:Binding Sites; D004355:Drug Stability; D004492:Edetic Acid; D004553:Electric Conductivity; D004926:Escherichia coli; D006358:Hot Temperature; D009691:Nucleic Acid Denaturation; D009698:Nucleoproteins; D011485:Protein Binding; D011489:Protein Denaturation; D013816:Thermodynamics
D009698:Nucleoproteins; D004492:Edetic Acid