Divalents separation affected

A second class of gels shows sudden volume changes with small changes in temperature. These gels are affected relatively little by changes in pH, ionic strength, and divalent ion concentration. As a result, they are much more suitable for chemical separations, and have been the major focus of our research. 

The factors that affect phase separation discussed in this section include anion effect, divalent effect, alkaline effect, mixing effect of interstitial flow, and the synergy of mixed surfactants. 

The presence of calcium ion also affects the power-law index. Figure 12 shows that higher power-law index values were obtained with the calcium ion, i.e., divalent ions enhance Newtonian behavior. It should be mentioned that there was no phase separation due to the presence of the calcium ion [9,55]. This is presumably due to the temperature (20°C) and the degree of hydrolysis of the polymer examined (0.28). 

The mobilities of proteins and protein complexes are affected both by the composition of the electrode buffer (concentration, pH, and presence or absence of divalent cations) and by the composition of the sample. Precise formulation of the electrode buffer is essential to obtain reproducible separations. While satisfactory separations can be obtained even with fairly high (up to 0.4 M) salt concentrations in the sample, high salt concentrations in a sample can significantly reduce the mobilities of proteins in that lane. Thus, where small differences in mobility are important, the concentrations of salt and buffer should be identical in all samples. 

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