Peptide Maps of Porcine Pepsin Prepared Using Soluble and Immobilized α-Chymotrypsin

Abstract

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