Interaction Between Crosslinked Polyelectrolytes and Dipolar Ions

2 Interaction between Crosslinked Polyelectrolytes and Dipolar Ions 

This behavior has been observed to a certain extent for some proteins at a low ionic strength of the solution. In contrast to this mechanism, in buffer systems 

High sorption capacities with respect to protein macromolecules are observed when highly permeable macro- and heteroreticular polyelectrolytes (biosorbents) are used. In buffer solutions a typical picture of interaction between ions with opposite charges fixed on CP and counterions in solution is observed. As shown in Fig. 13, in the acid range proteins are not bonded by carboxylic CP because the ionization of their ionogenic groups is suppressed. The amount of bound protein decreases at high pH values of the solution because dipolar ions proteins are transformed into polyanions and electrostatic repulsion is operative. The sorption maximum is either near the isoelectric point of the protein or depends on the ratio of the pi of the protein to the pKa=0 5 of the carboxylic polyelectrolyte [63]. It should be noted that this picture may be profoundly affected by the mechanism of interaction between CP and dipolar ions similar to that describedby Eq. (3.7). 

Since the mechanism of interaction between proteins polyfunctional with respect to ionogenic groups and CP is complex, an approximate method of calculation of sorption selectivity constants according to the inverse form of Langmuir isoterm should be used. Hence, the approximate values of AG, AH and AS obtained from Eq. (3.5) should be applied (Table 7). 

Calculations were usually carried out under the conditions of a pH-maximum of protein bonding. The experimental results show that the interaction of proteins and most other complex organic substances with CP is accompanied by an increase in the entropy of the system. 

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