Abstract
Quantities of serum albumin, papain, chymotrypsin, trypsin and polyvalent natural trypsin inhibitor antilysin coupled to 3-(2′,3′-epoxypropoxy)propyl-glass, 3-(2′,3′-epoxypropoxy)propyl-silica, epoxyactivated Sepharose 6B, glycidyl methacrylate copolymer and oxirane-acrylic beads (Röhm Pharma) were determined as a function of pH of the reaction mixture. Optimal coupling pH and the amounts of attached individual proteins were considerably affected by both the nature of the coupled protein and the nature of the solid matrix. In some cases the effect of increased ionic strength was studied. Differences in plots of the dependence of the amount of the coupled protein on pH and ionic strength are discussed in respect to the differences of isoelectric points, hydrophobicity and charge distribution of proteins and supports.
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