Adsorption characteristics of lysozyme on silochrome at different pH values

It is established that the adsorption of lysozyme on silochrome proceeds by a two-stage scheme that includes equilibrium adsorption and irreversible multipoint binding, complicated by the association of surface protein. It is shown that, a substantial change in the mechanism of adsorption occurs in dependence on pH. The density of the monolayer increases with increasing pH in the range of 6?C10. The rate constants of adsorption and sites occupied by a molecule of protein at different pH values are calculated.