Peptide maps of porcine pepsin prepared using soluble and immobilized alpha-chymotrypsin.

Reverse-phase high performance liquid chromatography (RP-HPLC) was used for characterization of peptide maps of porcine pepsin using soluble or immobi lized alpha-chymotrypsin. The immobilized enzyme was prepared by its coupli ng to periodate-oxidized poly(acrylamide-co-allyl alpha-D-galactoside or al lyl beta-lactoside) copolymer (O-glycosylated acrylamide copolymer). After sodium cyanoborohydride reduction, a stable linkage was formed. Specific ac tivity of alpha-chymotrypsin, linked to the copolymer containing bound alph a-D-galactosyl or beta-lactosyl residues was 59.1 or 314.4% activity of sol uble enzyme.