1983
DOI: 10.1016/0032-3950(83)90303-9
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Interaction of protein molecules with a network polyelectrolyte in solution

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Cited by 5 publications
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“…Systems containing both weak polyelectrolytes and biopolymers have been studied in the context of protein separations: Morawetz (19), Glatz (20), and others (21) studied the phase separation of proteins with homo-and co-polymers of acrylic (AA) and methacrylic acid (MA). Related studies describe soluble complex formation between such polyacids and proteins (22), and binding of proteins to crosslinked acrylic acid copolymers (23). Fleer and coworkers (24) studied the adsorption of PAA onto cationic latexes.…”
Section: Introductionmentioning
confidence: 99%
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“…Systems containing both weak polyelectrolytes and biopolymers have been studied in the context of protein separations: Morawetz (19), Glatz (20), and others (21) studied the phase separation of proteins with homo-and co-polymers of acrylic (AA) and methacrylic acid (MA). Related studies describe soluble complex formation between such polyacids and proteins (22), and binding of proteins to crosslinked acrylic acid copolymers (23). Fleer and coworkers (24) studied the adsorption of PAA onto cationic latexes.…”
Section: Introductionmentioning
confidence: 99%
“…The primary issue in such comparisons has been of course the variable charge density of weak polyelectrolytes and their concomitant pH-dependence, but it has also been pointed out that the pK of ionizable groups of weak polyions may be perturbed by the colloid surface potential. Fleer et al (23) commented on the need to distinguish between the adsorption of strong and weak polyelectrolytes, and found that the effect of ionic strength on adsorption was far lower for weak polyelectrolytes. Shatayeva (33) discussed the relative binding of proteins to weak and strong cation exchange resins in terms of the acid strength of the network ionophores.…”
Section: Introductionmentioning
confidence: 99%