Dependence of Salt Concentration on Glycosaminoglycan–Lysozyme Interactions in Cartilage

Viscosity and Wettability of Hyaluronic Acid according to Antimicrobial Supplementation, Ionic Strength, and pH

“…High binding affinity was previously confirmed at approximately 10-50 mM salt and at pH 7.5. [6][7][8] It has also been reported that the myeloperoxidase activity was not affected by the formation of HA-myeloperoxidase ionic complex, 9,12) which was in consistent with our pervious study using bLPO.…”

“…The previous reports has already suggested the formation of complex molecules between HA and lysozyme [6][7][8] and between HA and peroxidase. in DDW and 0.5 mg/mL in SSB, to verify the influence of ionic strength on viscosity and wettability.…”

“…Some reports have suggested an ionic interaction between HA and lysozyme or peroxidase. [6][7][8][9] It has been previously reported that HA inhibited lysozyme activity of leucocytic lysosome by 30%.…”

Interaction between lysozyme and poly(acrylic acid) microgels

“…However, in the complexation of proteins with linear polymers, such nonmonotonic ionic strength dependence with optima in the ionic strength range 5-30 mM has been observed before, both for protein-polymers pairs of identical [42] and opposite [42,43] charge. It has been suggested that above this optimum, an ionic strength increase primarily screens the attractive interactions, whereas at ionic strengths below optimum, an increase in ionic strength primarily screens repulsive interactions [42].…”

β-Lactoglobulin (BLG) binding to highly charged cationic polymer-grafted magnetic nanoparticles: Effect of ionic strength

“…However, it is interesting to note several recent reports of non-monotonic ionic strength dependence of the binding constant for some protein-polyelectrolyte systems. For example, interaction pairs including BSA-PDADMAC, BLG-PDADMAC [15], BLG-pectin coacervates [16], lysozyme/ chondroitin sulfate and lysozyme/hyaluronic acid [17] were all found a maximum in the protein-polyelectrolyte binding affinity in the same ionic strength range of 10-30 mM. Dubin and co-workers [18] chose highly divergent systems include heparin-bovine serum albumin, heparin-insulin, and bovine serum albumin with hydrophobically modified poly(acrylic acid) (HMPAA) to understand the cooperative effects between long range repulsions and short range attractions (LRSA effect).…”