Abstract
A study has been made of the bonding of proteins (serum albumin, haemoglobin, chymotrypsinogen) to carboxylic macronetwork cationites synthesized from methacrylic acid and ethylenedimethacrylamide. It was found that a change in the degree of ionization of the cationites in the range α = 0·15−0·4 involving breakdown of the secondary structure of polymethacrylic acid chains between chemical crosslinks in the network, results in an increased sorptive capacity of the proteins, reaching a maximum at α = 0·35. The sorption of proteins on carboxylic cationites has been investigated for two degrees of ionization ( α = 0 and 0·4), where polymer chains of the network structure are in different conformational states. The cooperative character of the sorption isotherms was observed for proteins on the nonionized form of the cationite, when the PMAA chains are tighly packed into a secondary structure; the usual type of Langmuir isotherm appears when α = 0·4.
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