Collect. Czech. Chem. Commun. 1999, 64, 710-716

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

Hana Vaňkováa,*, Zdenka Kučerováa and Marie Ticháb

a Institute of Pathophysiology, 1st Faculty of Medicine, Charles University, 128 53 Prague 2, Czech Republic
b Department of Biochemistry, Charles University, 128 40 Prague 2, Czech Republic


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.

Keywords: Immobilization; α-Chymotrypsin; Peptide maps; Reverse-phase HPLC; Porcine pepsin; Proteins; Enzymes.